ライフサイエンスコーパス: F1-ATPase

1 ns and the other motor proteins (myosins and F1-ATPase).

2 r to the ATPase domains of helicases and the F1 ATPase.

3 d ATP8 genes is translationally regulated by F1 ATPase.

4 e of counterclockwise rotation driven by the F1-ATPase.

5 th F1-depleted membrane vesicles for binding F1-ATPase.

6 directly proportional to its ability to bind F1-ATPase.

7 sites, were introduced into Escherichia coli F1-ATPase.

8 the P-loop in the beta-subunit of the yeast F1-ATPase.

9 utilization and transduce this demand to F0-F1-ATPase.

10 maging and rotor manipulation experiments on F1-ATPase.

11 the gamma-subunit on free energy surfaces of F1-ATPase.

12 ic beta subunits of the bovine mitochondrial F1-ATPase.

13 the binding interactions of the b dimer with F1-ATPase.

14 in the betaTP and betaDP catalytic sites of F1-ATPase.

15 concerning the various structures of bovine F1-ATPase.

16 h mutation of the analogous catalytic Glu in F1-ATPase.

17 ntitative structure-function correlation for F1-ATPase.

18 core is also found within helicases and the F1-ATPase.

19 uable for future transition state studies of F1-ATPase.

20 ls to cilia, where they may interact with F0/F1 ATPases.

21 feature of the binding change mechanism for F1-ATPases.

22 those of active mitochondrial and bacterial F1-ATPases.

23 likewise closely similar to those of active F1-ATPases.

24 resolution density to be interpreted as the F1-ATPase, a central and a peripheral stalk and an FO me

25 ent results provide a rationalization of how F1-ATPase achieves the coupling between the small change

26 ese strains had readily detectable levels of F1-ATPase activity and proton pumping activity.

27 ehydrogenase, triosephosphate isomerase, and F1 ATPase, alpha subunit).

28 utarate dehydrogenase, and the mitochondrial F1-ATPase alpha1 subunit.

29 kinetic model for the mechanism of action of F1-ATPase and demonstrate the role of different protein

30 The F1-ATPase and F1-zeta models of P. denitrificans were su

31 Here we use a coarse-grained model of F1-ATPase and generate, without the adjustment of phenom

32 cA is structurally homologous to that of the F1-ATPase and helicases.

33 rho shares a common structural core with the F1-ATPase and other hexameric helicases, there has been

34 Like the F1-ATPase and ring helicases, RecA forms a hexameric rin

35 opose that the rho hexamer is similar to the F1-ATPase and T7 DNA helicase-containing noncatalytic si

36 ly believed that MgATP2- is the substrate of F1-ATPases and ATP4- acts as a competitive inhibitor.

37 lysis of ATP by a single beta subunit within F1-ATPases and implicate alanine 158 as residing very ne

38 t catalytic site, and hydrolytic activity in F1-ATPases and that these three properties are strongly

39 g at alanine 158, a conserved residue within F1-ATPases and the third residue within the nucleotide b

40 f V1-ATPases that are distinct from those of F1-ATPases and will further our understanding of the gen

41 such as F1-adenosine triphosphate synthase (F1-ATPase) and myosin are similar in size, and they gene

42 tant for ATP hydrolysis catalyzed by soluble F1-ATPase, and the latter four residues were also very i

43 ow parallels between the MCM complex and the F1-ATPase, and we discuss how ATP hydrolysis by the MCM

44 he alpha- and beta-subunits of mitochondrial F1-ATPase are folded into beta-barrel domains and were p

45 nd release rate constants for nucleotides in F1-ATPase as a function of the rotor angle is further ex

46 nfirmed binding of the modified b mutants to F1-ATPase as well as to F1-delta.

47 The final models show that zeta enters into F1-ATPase at the open catalytic alphaE/betaE interface,

48 Previous studies have shown that the F1-ATPase beta-subunit precursor (pre-F1beta) of the yea

49 Levels of the mitochondrial protein F1-ATPase beta-subunit were not decreased to a similar d

50 Beta-Arg-182 in Escherichia coli F1-ATPase (beta-Arg-189 in bovine mitochondrial F1) is a

51 for ANT isoform1 and the beta subunit of the F1-ATPase (betaF1) were analyzed in myocardium remote fr

52 Two mutants of the Escherichia coli F1 ATPase, betaY331W:E381C/epsilonS108C and alphaS411C/b

53 unit dimer may be a necessary step preceding F1-ATPase binding in the assembly of the enzyme complex.

54 hree components: an engineered substrate, an F1-ATPase biomolecular motor, and fabricated nanopropell

55 teractions with five of the nine subunits of F1-ATPase but mainly with the beta(DP)-subunit.

56 ete inactivation of the bovine mitochondrial F1-ATPase by Al3+, F-, Mg2+, and excess ADP occurs as AD

57 ted F1 but reduced the maximal inhibition of F1-ATPase by from >90% to approximately 20%.

58 r proteins, including kinesins, myosins, and F1-ATPases, by using a version of the simple elastic-net

59 that four of the five bovine subunits of the F1-ATPase can be imported and function in an otherwise y

60 ment of the adenosine triphosphate synthase (F1-ATPase) can function as an ATP-fuelled rotary motor a

61 ted close to the gamma-phosphate of MgATP in F1-ATPase catalytic sites, were investigated.

62 immediately preceding the P-loop sequence in F1-ATPase catalytic sites.

63 A model of the F1-ATPase catalytic transition state structure is presen

64 The yield of chloroplast F1-ATPase (CF1) purified from thylakoids was unaltered,

65 Mg2+-ATPase activity of purified chloroplast F1-ATPase (CF1).

66 es were performed on reconstituted 3-subunit F1-ATPase (-delta epsilon) from Escherichia coli and bot

67 In the structure of the rat liver F1-ATPase, determined to 2.8-A resolution in the presenc

68 nt to create clockwise torque that overcomes F1 ATPase-driven counterclockwise torque at high ATP is

69 Levels of membrane-associated F1-ATPase dropped precipitously for the longer deletions

70 bsol Ala-79-->Leu, were shown to elute with F1-ATPase during size exclusion chromatography, suggesti

71 In human F1-ATPase, each 360 degrees rotation consists of three 1

72 three beta subunits of the Escherichia coli F1 ATPase (ECF1) have been explored in relation to the i

73 ite occupation for both the Escherichia coli F1-ATPase (EcF1) and Thermophilic Bacillus PS3 F1-ATPase

74 ion of the bacterial flagellar motor and the F1-ATPase enzyme.

75 es resemble the known structures of RecA and F1-ATPase enzymes.

76 F1-ATPase (F1) is the catalytic portion of ATP synthase,

77 altered bsol polypeptides for competing with F1-ATPase for binding to F1-depleted membrane vesicles.

78 In the structure of the F1-ATPase from C. thermarum, ATP and a magnesium ion are

79 unit (-delta epsilon) and 4-subunit (-delta) F1-ATPase from chloroplasts.

80 Escherichia coli F1-ATPase from mutant betaY331W was potently inhibited b

81 In contrast to the F1-ATPases from bovine mitochondria and the thermophilic

82 the epsilon subunit of the Escherichia coli F1-ATPase has been determined by NMR spectroscopy.

83 and epsilon subunits in the Escherichia coli F1-ATPase have been explored by a combination of cross-l

84 hange mechanism of rotary catalysis by which F1-ATPase hydrolyzes ATP has been supported by equilibri

85 onine in the beta-subunit of the chloroplast F1-ATPase in Chlamydomonas (betaT168).

86 able to import, assemble subunits of bovine F1-ATPase in mitochondria and form a functional chimeric

87 alt counterclockwise rotation powered by the F1-ATPase in steps equivalent to the rotation of single

88 ligands from water to the different sites of F1-ATPase in their different conformational states.

89 ons, using betaY331W mutant Escherichia coli F1-ATPase, in which the genetically engineered tryptopha

90 nt of a kinetic scheme for ATP hydrolysis by F1-ATPase, in which the rate constants are associated wi

91 Another structure, described here, of bovine F1-ATPase inhibited by an ATP analog and the phosphate a

92 ially identical, and the structure of bovine F1-ATPase inhibited by IF1 represents the catalytic dwel

93 The structure of bovine F1-ATPase inhibited with ADP and beryllium fluoride at 2

94 ha(E)beta(E)-catalytic interface, whereas in F1-ATPase inhibited with IF1, the equivalent site is cha

95 In a known structure of bovine F1-ATPase inhibited with residues 1-60 of IF1, the inhib

96 The F1-ATPase inhibitor protein, IF1, halts the rotary cycle

97 F1-ATPase is a highly efficient molecular motor that can

98 The F1-ATPase is a multimeric enzyme (alpha3 beta3 gamma del

99 The F1-ATPase is a multimeric enzyme composed of five subuni

100 F1-ATPase is an ATP-driven rotary motor in which a rod-s

101 The rotation of the central stalk of F1-ATPase is driven by energy derived from the sequentia

102 F1-ATPase is the catalytic complex of rotary nanomotor A

103 F1-ATPase is the catalytic component of the ATP synthase

104 nd torque (rotation of the gamma-subunit) in F1-ATPase is very challenging.

105 atalysis at each subunit, similar to that of F1 ATPase, is supported by these results.

106 hese models (and others) were tested with an F1- ATPase, isolated from Halobacterium saccharovorum, b

107 The morphology of F1-ATPases lacking one or more small subunits has been i

108 In this mechanism, an F1-ATPase-like rotational movement around the single-str

109 lucidated the full chemo-mechanical cycle of F1-ATPase, mostly based on F1 from thermophilic bacteria

110 esign, construction and analysis of a mutant F1-ATPase motor containing a metal-binding site that fun

111 nucleotide-exchange steps in the myosin and F1-ATPase motors and inform how the two heads of a kines

112 together with characteristics of a group of F1 ATPase mutant enzymes and were analyzed quantitativel

113 est-frequency modes (one for myosin, two for F1-ATPase) obtained from normal-mode analysis of the ela

114 blocks rotation of the gamma subunit of the F1-ATPase of P. denitrificans by a hitherto unknown quat

115 Heterologous inhibition of the F1-ATPase of P. denitrificans by the mitochondrial IF1 s

116 Steady-state ATP hydrolysis in the F1-ATPase of the F(O)F1 ATP synthase complex involves ro

117 their reactivity with antibodies against the F1 ATPase purified from C. thermoautotrophicum and by co

118 a, beta, gamma, and epsilon, constituted the F1-ATPase purified from the latter bacterium.

119 henyl)adenosine 5'-triphosphate (TNP-ATP) by F1-ATPase required filling of only two catalytic sites o

120 he adenine nucleotide translocator (ANT) and F1-ATPase respectively regulate mitochondrial adenosine

121 The recently determined structure of the F1-ATPase reveals a direct correspondence between the ty

122 The structure of yeast F1-ATPase reveals that the mgi residues cluster around t

123 tained from other molecular machines such as F1 -ATPase, RNA polymerase, or topoisomerase.

124 ecordings of other single molecules, such as F1-ATPase, RNA polymerase, or topoisomerase, have the sa

125 wn insights into the molecular nature of the F1-ATPase rotary motor.

126 torque-driven gamma-subunit rotation in the F1-ATPase rotary motor.

127 we analyzed protein-protein interactions in F1-ATPase, Sec23p/Sec24p, DNA-directed RNA polymerase an

128 The crystal structure of bovine F1-ATPase shows that these suppressor residues are locat

129 recent x-ray structure of the mitochondrial F1 ATPase, site-directed mutagenesis of the yeast VMA2 g

130 A model for F1-ATPase steady-state turnover is presented that encomp

131 hanges in Pi protonation, and changes of the F1-ATPase structure in the 40 degrees substep.

132 d reaction pathway between PcrA helicase and F1-ATPase suggest a similar mechanochemical mechanism at

133 er atp22 mutants have oligomycin-insensitive F1-ATPase, suggesting that the lesion is confined to F0.

134 -ATPase (EcF1) and Thermophilic Bacillus PS3 F1-ATPase (TF1), which have different behavior.

135 F1-ATPase, the catalytic complex of the ATP synthase, is

136 F1-ATPase, the catalytic domain of ATP synthase, synthes

137 During mitochondrial ATP synthesis, F1-ATPase-the portion of the ATP synthase that contains

138 tudy that used a coarse-grained model of the F1-ATPase to generate a structure-based free energy land

139 netics of Mg x ATP hydrolysis in the soluble F1-ATPase upon rapid filling of all three catalytic site

140 he three catalytic sites of Escherichia coli F1-ATPase was investigated, using a genetically engineer

141 ns in the catalytic site of Escherichia coli F1-ATPase was investigated.

142 E204Q in the beta subunit of the chloroplast F1-ATPase was made by biolistic transformation of Chlamy

143 he three catalytic sites of Escherichia coli F1-ATPase was measured in the presence of the inhibitors

144 sidue alpha-Arg-376 in the catalytic site of F1-ATPase was studied.

145 ng for the beta subunit of the mitochondrial F1-ATPase, was cloned from nine independent isolates of

146 The F1F0 ATP synthase is composed of the F1-ATPase which is bound to F0, in the inner membrane of

147 of one conformation of the catalytic moiety F1-ATPase, whose structure is known from crystallography

148 In the structure of F1-ATPase with five bound ADP molecules (three in alpha-

149 Inactivation of MF1 (bovine mitochondrial F1-ATPase) with 5'-p-fluorosulfonylbenzoylethenoadenosin