ライフサイエンスコーパス: MgADP

1 MgADP binding to HMM decreases mu(e) to -0.57 (microm/s)

2 MgADP binding to the allosteric site enhances the affini

3 purified BeFx complex contained 3.8 +/- 0.1 MgADP per mol Kp1.

4 se in intensity over those observed with 1:1 MgADP.

5 The F(1).MgADP.ScFx complex mimics a catalytic transition state.

6 nalog (TSA) components taurocyamine-NO3 (2-)-MgADP.

7 of MgADP-berellium fluoride (BeF(X)) (31%), MgADP-AlF(4)(-) (31%), MgATP (36%), and MgADP (30%) comp

8 Both R72E and T125A displayed a MgADP-dependent decrease in k(cat) but no MgADP-dependen

9 ndent K-type activation but also displayed a MgADP-dependent decrease in k(cat).

10 n in SUR1 or SUR2B (but not SUR2A) abolished MgADP activation completely.

11 The activator, MgADP, also altered the affinity of fructose 6-phosphate

12 The potentiation of tension with 4 mM added MgADP was 20-25% at low temperatures (approximately 5-10

13 uxley-Simmons phase 2) was slower with added MgADP.

14 increased approximately 20% with 4 mM added [MgADP].

15 Localization of mutations that alter MgADP activation near the transferred phosphate group in

16 n indicate that the transition state analog, MgADP-aluminum fluoride-acetate, forms an abortive compl

17 1%), MgADP-AlF(4)(-) (31%), MgATP (36%), and MgADP (30%) compared with the nucleotide-free environmen

18 ATP and MgADP regulate K(ATP) channel activity and hence potenti

19 rporated equations for intracellular ATP and MgADP regulation of the K(ATP) current and MgATP regulat

20 orescence quenching induced by ADP, ATP, and MgADP is biphasic, revealing two classes of binding site

21 tions on KATP channels, with ATP closing and MgADP opening the channel.

22 t this, we measured cross-bridge cycling and MgADP release rates in skinned soleus fibers using stoch

23 e strongly bound rigor (nucleotide-free) and MgADP states, actin offered no protection from solvent q

24 elevation of inorganic phosphate (P(i)) and MgADP on steady-state force and stiffness were examined.

25 e effects of MgATP, phosphate (P, P(i)), and MgADP were studied on three exponential processes by sin

26 pendent changes in cross-bridge kinetics and MgADP release that are separate from, or complementary t

27 Remarkably, MgAMP and MgADP but not MgATP protected PFK-1 against inhibition b

28 nt 1(S1) with the bound MgADP, MgAMPPNP, and MgADP.BeF(x) provide crystallographic evidence for a des

29 with magnesium pyrophosphate, MgAMPPNP, and MgADP.vanadate have been determined.

30 Mutant E552A/E1197A bound MgATP and MgADP (1 mol/mol) with K(d) 9.2 and 92 microm, showed st

31 ants showed lower stoichiometry of MgATP and MgADP binding, in the order Ala > Gln > Asp > Lys.

32 g and equal dissociation rates for MgATP and MgADP.

33 se MDR3 P-glycoprotein and natural MgATP and MgADP.

34 ors of K(ATP) channel activity are MgATP and MgADP.

35 monitor the effect of HscA, HscB, MgATP, and MgADP on the time course of cluster transfer from [2Fe-2

36 The MgATP- and MgADP-induced conformational changes in BchL were examin

37 analogue complex with arginine, nitrate, and MgADP, was nearly identical to wild type.

38 s a coupling free energy between Fru-6-P and MgADP of -1.56 kcal/mol under these conditions, indicati

39 upports the conclusion that although PEP and MgADP bind to the same site, they do not use the same co

40 pecifically, phospho(enol)pyruvate (PEP) and MgADP binding to the mutant PFK can be directly observed

41 Furthermore, both phosphoenolpyruvate and MgADP act by influencing the fast complex formation step

42 tial release of inorganic phosphate (Pi) and MgADP.

43 Here we examine rundown and MgADP activation of wild-type and Kir6.2-F333I/SUR2A cha

44 y with SUR2A to modulate channel rundown and MgADP activation.

45 g the adjacent residue, G334, on rundown and MgADP activation.

46 In contrast, rundown and MgADP reactivation of wild-type and Kir6.2-G334D/SUR2A c

47 R176 and R177 with C166A, sulphonylurea and MgADP sensitivities were restored.

48 (P(o)), PIP2 affinity, and sulphonylurea and MgADP sensitivity.

49 8), leads to defects in both trafficking and MgADP response of K(ATP) channels.

50 but before MgADP release, whereas in aorta, MgADP release is associated with a portion of the cross-

51 -jump-induced tension rise became slower as [MgADP] was increased, with half-maximal effect at 0.5 mM

52 rescued to the cell surface have normal ATP, MgADP, and diazoxide sensitivities, demonstrating that S

53 ression level and normal sensitivity to ATP, MgADP, and diazoxide.

54 urface exhibited WT-like sensitivity to ATP, MgADP, and diazoxide.

55 utant was slightly inhibited by MgADP-azide, MgADP-fluoroaluminate, or MgADP-fluoroscandium, in contr

56 rently with or after P(i) release but before MgADP release, whereas in aorta, MgADP release is associ

57 ysis of the three-ligand interaction between MgADP, Fru-6-P, and MgATP.

58 ucture of human RFK cocrystallized with both MgADP and FMN.

59 PA containing bound MgADP supports elongation of the actin filament barbed e

60 E2P form (PDB code 1wpg) that contains bound MgADP.

61 MgAMP hydrolysis) replaced part of the bound MgADP although four AlF(4)(-) ions were retained, demons

62 llop myosin subfragment 1(S1) with the bound MgADP, MgAMPPNP, and MgADP.BeF(x) provide crystallograph

63 the alpha(TP)-beta(TP) interface with bound MgADP in crystal structures represents a catalytic site

64 f the protein has been determined with bound MgADP to 1.6 A resolution.

65 recombinant BchL was crystallized with bound MgADP, and the structure was determined to 1.6 A resolut

66 channel activity via a PIP2-independent, but MgADP-dependent process.

67 bited by MgATP (>50 microM) and activated by MgADP (200 microM).

68 eins retained the ability to be activated by MgADP and inhibited by phosphoenolpyruvate (PEP).

69 he SUR1-D860A mutation were not activated by MgADP in either the presence or absence of MgATP.

70 c normally but are unable to be activated by MgADP.

71 The free energy of activation by MgADP for this heterotropic interaction is -0.58 kcal/mo

72 extent of macroscopic current activation by MgADP was unaffected.

73 onductance, block by MgATP and activation by MgADP, did not differ between these two locations.

74 mice, due to impaired channel activation by MgADP.

75 anding the allosteric activation of EcPFK by MgADP has been complicated by the complex web of possibl

76 l basis of allosteric activation of EcPFK by MgADP is complicated by the multiplicity of binding site

77 alphaS347A mutant was slightly inhibited by MgADP-azide, MgADP-fluoroaluminate, or MgADP-fluoroscand

78 type, ATPase of mutants was not inhibited by MgADP-fluoroaluminate or MgADP-fluoroscandium, showing t

79 f MgADP and MgATPgammaS but was inhibited by MgADP.V(i) and actin.

80 the wild-type protein, but its inhibition by MgADP was unchanged, indicating that MgADP binding is no

81 tained, demonstrating that full occupancy by MgADP is not required for the stability of the complex.

82 Channel regulation by MgADP is dependent on nucleotide interaction with the cy

83 egion of Fru-6-P in allosteric regulation by MgADP.

84 itivity and do not respond to stimulation by MgADP or diazoxide.

85 plete in <0.5 ms), the increase of force by [MgADP] was not associated with a concomitant increase of

86 AIR), MgATP, and bicarbonate into N(5)-CAIR, MgADP, and P(i).

87 eric site of PFK (i.e., mutant E187A) causes MgADP to lose its allosteric effect upon Fru-6-P binding

88 s, and to show that the formation of a ChlID-MgADP complex, mediated by the arginine finger and the s

89 around 109 pN for formation of single ChlID-MgADP complexes.

90 actors that stabilize formation of the ChlID-MgADP complex at the single molecule level; ChlD was att

91 se it does not promote the formation of a CK.MgADP.anion.creatine transition-state analogue complex (

92 various monovalent anions in forming the CK.MgADP.anion.creatine TSAC.

93 ding cassette (ABC) transporter that confers MgADP stimulation to the channel.

94 when at least two catalytic sites contained MgADP.

95 channel types responded to the diphosphates MgADP and MgGDP.

96 esponsive to channel activators such as DZX, MgADP and metabolic inhibition.

97 om bi bi kinetic mechanism, for which both E-MgADP-FAK-tide and E-MgATP-P-FAK-tide dead-end complexes

98 slow kinetic step follows formation of the E-MgADP-P-FAK-tide complex.

99 t meglitinide binding to SUR1 impairs either MgADP binding or the transduction pathway between the NB

100 id not show an allosteric response to either MgADP or PEP.

101 en and the closed conformations, with either MgADP or MgATP at the active site.

102 orescence spectrum observed after entrapping MgADP-fluoroaluminate complexes in two catalytic sites o

103 ADP and promotes the formation of the enzyme*MgADP*nitrate*creatine TSAC.

104 e observed decreases in binding affinity for MgADP and PEP in LbPFK as compared to the other two enzy

105 and nitrate increases the affinity of CK for MgADP and promotes the formation of the enzyme*MgADP*nit

106 ring titration reduces the apparent K(d) for MgADP 10-fold to 13.7 +/- 0.7 microM, and Delta%F increa

107 ncentrations of NaNO3, the apparent K(d) for MgADP decreases with increasing fixed concentrations of

108 atine, but no nitrate, the apparent K(d) for MgADP remains essentially unchanged at 132 +/- 10 microM

109 A plot of the apparent K(d) for MgADP vs [NO3-] suggests a K(d) for nitrate from the TSA

110 se in binding affinity of acetate kinase for MgADP in the presence of AlCl(3), NaF, and acetate.

111 of various anions, apparent K(d) values for MgADP of 132 +/- 10 microM, 25.2 +/- 1.3 microM, 18.8 +/

112 affinity catalytic site, the K(d) values for MgADP, ADP, and ATP equal 10, 43, and 185 nM, respective

113 ing the initial stages of complex formation, MgADP bound to the complexed Kp2 in a manner similar to

114 the complexes GKy.MgATP, GKy.MgADP, and GKy.MgADP.[u-(13)C]GMP were determined by two-dimensional tr

115 ly constrained, two substrate complexes, GKy.MgADP.[u-(13)C]GMP, the guanyl glycosidic torsion angle,

116 ylate kinase in the complexes GKy.MgATP, GKy.MgADP, and GKy.MgADP.[u-(13)C]GMP were determined by two

117 tors, the primary force-generating state has MgADP tightly bound, whereas myosin is strongly bound to

118 For HMM(MgATPgammaS)(2) and HMM(MgADP.P(i))(2) the values of mu(e) are -0.077 and -0.17

119 , on the other hand, increases mu(e) for HMM(MgADP)(2) to values near those observed for the steady-s

120 sociates from HMM(MgADP.P(i))(2) to form HMM(MgADP)(2), mu(e) decreases to -0.61 (microm/s)/(V/cm).

121 When P(i) dissociates from HMM(MgADP.P(i))(2) to form HMM(MgADP)(2), mu(e) decreases to

122 rate the rate of MgADP release from acto-HMM-MgADP or slow its binding to acto-HMM.

123 However, MgADP activation of channel activity was abolished.

124 -NTPDase 8, the human E-NTPDase 8 hydrolyzes MgADP poorly and is inhibited by several detergents as w

125 For skinned muscle, an increase in MgADP or inorganic phosphate (Pi) should shift the distr

126 PFK does not follow the same pattern seen in MgADP activation of EcPFK.

127 erature, and the basic effects of increased [MgADP] on endothermic force, can be qualitatively simula

128 ening velocity was decreased with increased [MgADP] at low and high temperatures.

129 e activity is reduced 5-fold, and inhibitory MgADP entrapped in a catalytic site during turnover does

130 sents a catalytic site containing inhibitory MgADP.

131 ropensity of the enzyme to entrap inhibitory MgADP in a catalytic site during turnover.

132 nous nucleotides, does not entrap inhibitory MgADP in a catalytic site during turnover.

133 subcomplexes resist entrapment of inhibitory MgADP in a catalytic site during turnover.

134 turnover-dependent entrapment of inhibitory MgADP in a catalytic site, ATPase activity of the cross-

135 endency than wild type to release inhibitory MgADP entrapped in a catalytic site during turnover when

136 Intracellular MgADP modulated sulphonylurea block, enhancing inhibitio

137 nts in the presence of DZX and intracellular MgADP.

138 scheme: where A is actin, M is myosin, D is MgADP, and S is MgATP.

139 ial slow release of Mg (2+) from the kinesin-MgADP complex but strongly inhibit the fast release of M

140 with the rate proportional to the liberated [MgADP].

141 ding affinity toward the allosteric ligands, MgADP and PEP, with dissociation constants of approximat

142 R171E maintained MgADP-dependent K-type activation but also displayed a M

143 TP exchange between the cytosol and matrix, [MgADP]-dependent mitochondrial ATP synthase activity, an

144 investigated the interactions between MgATP, MgADP, and the sulphonylurea gliclazide with KATP channe

145 The effects of phosphate, MgATP, MgADP and Ca2+ were studied in Tm-reconstituted myocardi

146 uced K(ATP) current activation by 100 microM MgADP, whereas the S2R mutation in SUR1 or SUR2B (but no

147 incubation with stoichiometric or 200 microM MgADP irreversibly inactivated ATPase activity with a co

148 tion with stoichiometric MgADP or 200 microM MgADP irreversibly inactivated the steady state ATPase a

149 t is slowed 3-4-fold in the presence of 1 mM MgADP, but the distribution between the fast and slow (c

150 Addition of 2 mm MgADP induced a slightly greater blue shift and a slight

151 0-12 degrees C; the relation with added 4 mM MgADP was shifted upwards on the tension axis and toward

152 Photolysis of caged ADP to cause a 0.5 mM MgADP jump initiated an increase in isometric tension un

153 creased, with half-maximal effect at 0.5 mM [MgADP]; the pre- and post-T-jump tension increased appro

154 irst seen in an unusual 2.5-A scallop myosin-MgADP structure and described as corresponding to a prev

155 Neither MgADP nor MgATP-gamma-S could replace MgATP.

156 in the absence of added creatine or nitrate, MgADP has an apparent K(d) of 135 +/- 7 microM, and the

157 a MgADP-dependent decrease in k(cat) but no MgADP-dependent K-type effects.

158 Addition of MgADP and APS, which together promote the formation of a

159 Addition of MgADP to the bath increased isometric tension over a wid

160 In contrast, addition of MgADP, Mg-5'-adenylyl beta,gamma-imidophosphate (MgAMP-P

161 The effect of additions of MgADP to rigor cross-bridges could result from rotation

162 type isoforms, we found that the affinity of MgADP for alpha-S1 (100 muM) is ~ 4-fold weaker than for

163 t is changes in the concentration of ATP, of MgADP, or of other agents, which couples glucose metabol

164 The binding of MgADP also stabilizes loop 1 and loop 3 but makes loop 2

165 Binding of MgADP causes significant changes in the conformation and

166 Binding of MgADP to nucleotide-binding domain 2 (NBD2) is critical

167 , as in the wild-type enzyme, the binding of MgADP to the active site in the mutant competitively inh

168 esidue beta-Trp-148 observed upon binding of MgADP.ScFx or MgIDP.ScFx.

169 n of 20 mM as judged by the concentration of MgADP needed to displace it.

170 atory proteins increase the concentration of MgADP required to inhibit sliding.

171 t induced by changes in the concentration of MgADP.

172 The apparent second-order rate constant of MgADP binding was estimated as approximately 1.0 x 10(6)

173 simulation suggested that the desorption of MgADP at a rate of ~7 s(-1) was the rate-limiting step i

174 e conditions, indicating that the effects of MgADP are diminished by a homotropic activation equal to

175 1% with respect to the total free energy of MgADP/fructose 6-phosphate (Fru-6-P) activation in the c

176 Notably, ScFx caused large enhancement of MgADP binding affinity at both catalytic sites 1 and 2,

177 bserved for the binding and the influence of MgADP and PEP on the enzyme.

178 tion of oxaloacetate, the phosphorylation of MgADP by carbamoyl phosphate, and the bicarbonate-depend

179 ex has been shown to form in the presence of MgADP and AlF(4)(-).

180 scallop S1 was increased in the presence of MgADP and MgATPgammaS but was inhibited by MgADP.V(i) an

181 he presence of MgATP than in the presence of MgADP or absence of nucleotide, consistent with closure

182 in isometric contraction, in the presence of MgADP, and in rigor.

183 racting more than doubled in the presence of MgADP, and we show that the N-terminal AAA(+) domain of

184 In the presence of MgADP, cross-linking was greatly enhanced for all of the

185 d nucleotides was greater in the presence of MgADP-BeF(X), MgATP, or MgADP-AlF(4)(-) than MgADP.

186 ity of W512-MDE increased in the presence of MgADP-berellium fluoride (BeF(X)) (31%), MgADP-AlF(4)(-)

187 arn if this effect is related to the rate of MgADP dissociation from the acto-S1 cross-bridge head, t

188 atory proteins either accelerate the rate of MgADP release from acto-HMM-MgADP or slow its binding to

189 Tropomyosin slows the rate of MgADP release, thus increasing the time the motor spends

190 ically insignificant) slowing in the rate of MgADP release.

191 ffinity and accelerating the overall rate of MgADP release.

192 Photolytic release of MgADP (25-300 microM) from caged ADP in permeabilized to

193 of the wild-type enzyme promotes release of MgADP from the affected catalytic site.

194 (Q10 of approximately 4) and the release of MgADP occurs by a subsequent, slower, two-step mechanism

195 es an alternative explanation of the role of MgADP in the E187A mutant.

196 riments, designed to test the specificity of MgADP, photolysis of caged ADP in the absence of Mg(2+)

197 tations that either prevent stabilization of MgADP at NBD2 or ATP at NBD1.

198 he force generating state by substitution of MgADP for MgATP in maximum contracting solutions resulte

199 imately 116 and 76 times higher than that of MgADP and 6-hydroxymethylpterin, respectively.

200 cant effects, both positive and negative, on MgADP stimulation of K(ATP) channels in excised patches

201 slow (catch) components is not dependent on [MgADP].

202 solved in the presence of either Mg(2)ATP or MgADP and AIR.

203 severely impaired responses to diazoxide or MgADP.

204 as not inhibited by MgADP-fluoroaluminate or MgADP-fluoroscandium, showing the Arg side chain is requ

205 ed by MgADP-azide, MgADP-fluoroaluminate, or MgADP-fluoroscandium, in contrast to wild type and alpha

206 ordered substrate binding sequence (MgATP or MgADP before APS) as established from steady state kinet

207 exes is, however, not observed when MgATP or MgADP binds to the isolated Fe protein.

208 ith widely differing affinities for MgATP or MgADP.

209 e from Escherichia coli with either MgATP or MgADP/P(i) bound in the active site cleft.

210 r in the presence of MgADP-BeF(X), MgATP, or MgADP-AlF(4)(-) than MgADP.

211 are not involved significantly in MgATP- or MgADP-binding or in interdomain communication between ca

212 Activation by MgGDP (or MgADP) was similar for wild-type and mutant channels and

213 e mutant containing empty catalytic sites or MgADP bound to one catalytic site with CuCl(2) cross-lin

214 e close to 0.8, exhibits no sulphonylurea or MgADP sensitivity.

215 ase of Pi, and dissociation of the oxidized, MgADP-bound Fe protein from the MoFe protein.

216 ng phosphagen kinase reactions: phosphagen + MgADP + H(+) <--> guanidine acceptor + MgATP.

217 e, as tolbutamide was also unable to prevent MgADP activation of Kir6.2/SUR128 currents.

218 nally fast release of the hydrolytic product MgADP.

219 Retention of product MgADP is not the cause of reduced turnover.

220 s sensitivity to its physiological regulator MgADP.

221 a covalent Fhit-AMP intermediate and release MgADP.

222 The H249E mutation retained MgADP activation but did not respond to PEP.

223 ward (creatine phosphorylation) and reverse (MgADP phosphorylation) reactions.

224 lie in the same position as adenine in S1dC.MgADP.BeF(x), even though several of these nucleotide an

225 n of the fiber via dextran T-500, could slow MgADP release rate and increase cross-bridge attachment

226 vs. 2.0 mum sarcomere length due to a slower MgADP release rate (10.1 +/- 0.6 vs. 12.9 +/- 0.5 s(-1))

227 sarcomere length increased, due to a slower MgADP release rate (11.2 +/- 0.5 vs. 13.5 +/- 0.7 s(-1))

228 e observed in the presence of stoichiometric MgADP or MgAMP-PNP.

229 mutant after incubation with stoichiometric MgADP or 200 microM MgADP irreversibly inactivated the s

230 ting concentrations of the second substrate, MgADP.

231 MgADP-BeF(X), MgATP, or MgADP-AlF(4)(-) than MgADP.

232 ber of active channels in the patch and that MgADP reactivation involves recruitment of inactive chan

233 f the KATP channel and provide evidence that MgADP (or MgATP hydrolysis), acting at the regulatory su

234 We found that MgADP at low concentrations did not enhance or inhibit s

235 X-ray crystallographic data indicate that MgADP interacts with the conserved glutamate at position

236 ps and stiffness measurements indicated that MgADP increased mean force per cross-bridge at maximal C

237 tion by MgADP was unchanged, indicating that MgADP binding is not altered.

238 However, these authors later reported that MgADP inhibits Fru-6-P binding in the E187A mutant.

239 n the absence of citrate and CoA showed that MgADP was produced by both wild type and H760A forms of

240 Anisotropy shows that MgADP binding at the allosteric site occurred even when

241 occurs between isometric contraction and the MgADP states, i.e., during phosphate release.

242 steps of the cross-bridge cycle, such as the MgADP release rate.

243 Correspondingly, the MgADP release rate for alpha-S1 (350 s(-1)) is ~3-fold g

244 bstantially away from the active site in the MgADP-bound structure of MJ0796 compared with the ATP-bo

245 lar conformational effect is observed in the MgADP-bound structure of MJ1267, establishing the withdr

246 It is the MgADP complex that induces homotropic cooperativity in P

247 The structure of the MgADP-bound Fe protein provides important insights into

248 an effect that mimicked stabilization of the MgADP-bound posthydrolytic state at NBD2 by the gamma-ph

249 elative to the more compact structure of the MgADP-bound state.

250 For the structure of the MgADP/P(i) complex, crystals were grown in the presence

251 We report the MgADP structure of Yersinia enterocolitica YopO in compl

252 Similarly, the MgADP affinity (K(0)) was larger in type IID fibers than

253 ic linked-function analyses reveals that the MgADP complex modulates both the binding of the other th

254 Fe protein and flavodoxin revealed that the MgADP-bound state of the Fe protein has the most complem

255 In the MF(1) crystal structure with the MgADP-fluoroaluminate complex bound to two catalytic sit

256 e actin-binding cleft is closed, even though MgADP is tightly bound.

257 This increase was not induced by exposure to MgADP/P(i).

258 d with an SUR1 mutant that is insensitive to MgADP or MgATP activation.

259 three gain-of-function mutations, leading to MgADP hyperstimulation of the channel, are located in th

260 on the cell surface but failed to respond to MgADP even in the heterozygous state.

261 t SUR1 in COS cells have reduced response to MgADP ( approximately 10% that of the wild-type channels

262 UR2A largely confers a SUR1-like response to MgADP and meglitinide, whereas the reverse chimera (SUR1

263 ndent on hydrophobicity, channel response to MgADP is governed by multiple factors and involves the d

264 8L-SUR1 channel has increased sensitivity to MgADP and metabolic inhibition, decreased sensitivity to

265 ant K(ATP) channels that lack sensitivity to MgADP, expressed in COSm6 cells, we demonstrate that sim

266 the mutant channel complexes to tolbutamide, MgADP and diazoxide is disturbed.

267 educing the magnesium affinity of a myosin V-MgADP intermediate.

268 The two myosin V-MgADP states are of comparable energies, as indicated by

269 Two myosin V-MgADP states that are in reversible equilibrium, one tha

270 ng at the allosteric site occurred even when MgADP produced no allosteric effect.

271 y the mitochondrial ADP/ATP carrier, whereas MgADP is the substrate of ATP synthase (EC 3.6.3.14), th

272 401R mutation impairs the mechanism by which MgADP binding to NBD2 is translated into opening of the

273 We also clarify the mechanism by which MgADP produces an apparent increase of sulfonylurea effi

274 ely with a Hill number of 2.9 +/- 0.3, while MgADP binding is not cooperative.

275 i.e., a myosin isomerization associated with MgADP release for EMB and Pi release for IFI.

276 er slow muscle types, a step associated with MgADP release limits muscle contraction speed by delayin

277 On titration of CK with MgADP in the presence of 80 mM creatine and various fixe

278 alK from Pyrococcus furiosus in complex with MgADP and galactose has been determined to 2.9 A resolut

279 e crystal structures of RecA in complex with MgADP and MnAMP-PNP, a nonhydrolyzable analogue of ATP,

280 rin pyrophosphokinase (HPPK) in complex with MgADP has been determined at 1.5-A resolution with a cry

281 erium tuberculosis SK (MtSK) in complex with MgADP has been determined at 1.8 A resolution, revealing

282 termined in the apo form and in complex with MgADP.

283 mined structure of scallop S1 complexed with MgADP (which we interpret as a detached ATP state), reve

284 e of a nitrogenase complex crystallized with MgADP and MgAMPPCP, an ATP analogue.

285 egrees with MgATP, and 47 +/- 5 degrees with MgADP, which compares well to the 54 +/- 5 degrees publi

286 degrees with MgATP and 28 +/- 5 degrees with MgADP.

287 pen structure was energetically favored with MgADP at the active site, suggesting why only the open s

288 After ATP hydrolysis, with MgADP and MBP bound, the nucleotide-binding interface re

289 use Mdr3 P-glycoprotein upon incubation with MgADP and vanadate were studied along with the trapping

290 ATP hydrolysis conditions, intermediate with MgADP, and slowest with MgAMP-PNP.

291 der the temperatures studied for myosin with MgADP and the nucleotide-free myosin, raising the possib

292 proved with MgATP at low temperature or with MgADP or in the absence of nucleotide.

293 Furthermore, preincubation with MgADP and azide to inhibit F(1) or with high concentrati

294 has been determined at 2.7-A resolution with MgADP bound at its active site.

295 uscle creatine kinase (CK) was titrated with MgADP in 50 mM Bicine and 5 mM Mg(OAc)2, pH 8.3, at 30.0

296 hen the fluorescence of CK was titrated with MgADP in the presence of 80 mM creatine and fixed satura

297 Similarly, titration with MgADP in the presence of 10 mM NaNO3 and various fixed c

298 of the lowest affinity from titrations with MgADP and MgATP are 25 and 37 microM, respectively.

299 itrations of the introduced tryptophans with MgADP or MgATP revealed that both Mg-nucleotide complexe

300 es (GKy x MgATP) and 49 +/- 5 degrees (GKy x MgADP).