ライフサイエンスコーパス: lactose permease

1 -type enzyme IIAglc in a test for binding to lactose permease.

2 erase system inhibits transport catalyzed by lactose permease.

3 of a revised model for the structure of the lactose permease.

4 9 were mutagenized and tested for binding to lactose permease.

5 urface of enzyme IIAglc that interfaces with lactose permease.

6 and on proteoliposomes containing functional lactose permease.

7 a molecular chaperone in the assembly of the lactose permease.

8 g but not from PE-deficient cells expressing lactose permease.

9 tant interface between the two halves of the lactose permease.

10 at a step corresponding to deprotonation of lactose permease.

11 are unable to stabilize insertion of C6 from lactose permease.

12 a molecular hinge between the two halves of lactose permease.

13 s major facilitator transporter superfamily, lactose permease.

14 omparative structural model based on E. coli lactose permease.

15 permease PheP shares many similarities with lactose permease.

16 try of one mole of IIA(Glc) per six moles of lactose permease.

17 N-ethylmaleimide alkylation of single-Cys148 lactose permease.

18 eriplasmic domain or a cytoplasmic domain of lactose permease (a membrane protein).

19 port systems ("inducer exclusion"), and with lactose permease, a galactoside is required for unphosph

20 et al. described a one-step purification of lactose permease, a hydrophobic membrane transport prote

21 but quite distinct from those observed with lactose permease, a major facilitator superfamily member

22 To study this issue, lactose permease, a membrane transport protein from Esch

23 exploiting substrate protection of Cys148 in lactose permease, a methanethiosulfonate nitroxide spin-

24 among several ionizable residues within the lactose permease act in a concerted manner to control H+

25 ure at 3.5 angstroms of the Escherichia coli lactose permease, an intensively studied member of the m

26 ased on helical packing schemes proposed for lactose permease and Glut1 and predictions of secondary

27 s from Escherichia coli containing wild-type lactose permease and mutant Glu325 --> Ala.

28 ctroscopy has been performed on monodisperse lactose permease and on proteoliposomes containing funct

29 two well-studied MFS transporters, LacY (the lactose permease) and TetA (a tetracycline efflux protei

30 , is located in loop 2/3 and loop 8/9 in the lactose permease, and also in hundreds of evolutionarily

31 her biologic machines, such as ATP synthase, lactose permease, and G-protein-coupled receptors.

32 Lys358 (helix XI) form a salt bridge in the lactose permease, and neutral replacement of either resi

33 itution, topology, stability and function of lactose permease are found to have different dependences

34 Glu126 and Arg144 in the lactose permease are indispensable for substrate binding

35 and C-terminal six transmembrane domains of lactose permease are integrated into the membrane as sep

36 novel monodisperse, purified preparation of lactose permease, as well as functionally reconstituted

37 nteractions in the structure and function of lactose permease, Asp237 (helix VII), Asp240 (helix VII)

38 he crystal structure of the Escherichia coli lactose permease at 3.5 A with a bound substrate has bee

39 trate that the last two cytoplasmic loops in lactose permease comprise a discontinuous epitope for mo

40 By using site-directed chemical labeling of lactose permease, conformational changes induced by liga

41 Plasmids encoding "split" lactose permease constructs with discontinuities in eith

42 udied with Glu-126 and/or Arg-144 mutants in lactose permease containing a single, native Cys residue

43 nments that we tested, the expression of the lactose permease could be costly or beneficial, dependin

44 of beta-galactosidase from the cytoplasm of lactose permease-deficient E. coli ML-35.

45 By using functional lactose permease devoid of native Cys residues with a di

46 Furthermore, cell-free synthesis of lactose permease during DIB formation also results in ac

47 six C-terminal transmembrane helices (C6) in lactose permease, each containing a single Cys residue,

48 rminal six transmembrane helices (C6) of the lactose permease, each containing a single-Cys residue,

49 C-terminal six transmembrane helices (C6) of lactose permease, each with a single Cys residue, were c

50 The N- and C-terminal halves of lactose permease, each with a single-Cys residue in a cy

51 N- and C-terminal halves of lactose permease, each with a single-Cys residue in a pe

52 N and C-terminal halves of lactose permease, each with a single-Cys residue, were c

53 The lactose permease, encoded by the lacY gene of Escherichi

54 llar phosphatidylethanolamine lipids, lowers lactose permease folding and reconstitution yields but s

55 Crystal structures of lactose permease from Escherichia coli (LacY) exhibit tw

56 al structures of both a mutant and wild-type lactose permease from Escherichia coli (LacY) in an inwa

57 The structure of lactose permease from Escherichia coli in its lipid envi

58 litator Superfamily and is homologous to the lactose permease from Escherichia coli.

59 transmembrane alpha-helices, the full-length lactose permease from Escherichia coli.

60 Lactose permease from PE-containing membranes, but not f

61 available secondary transporter structures (lactose permease, glycerol-3-phosphate transporter) as w

62 The purification of monodisperse lactose permease has been aided by the development of a

63 The lactose permease has been expressed in contiguous, non-o

64 Previous analysis of this motif in the lactose permease has shown that the conserved glycine re

65 he results are consistent with the idea that lactose permease has two binding sites: one with higher

66 hemical, genetic, and biophysical studies on lactose permease have established its transmembrane topo

67 In the wild-type lactose permease, however, this motif has been evolution

68 Dephosphorylated IIA(Glc) binds directly to lactose permease in a reaction that requires binding of

69 e determined the topological organization of lactose permease in an Escherichia coli model cell syste

70 ar-dynamics simulations of membrane-embedded lactose permease in different protonation states, both i

71 ntiate the conclusion that regulation of the lactose permease in E. coli by the PTS is mediated by a

72 Lactose permease in Escherichia coli (LacY) transports b

73 ific role for PE in structural maturation of lactose permease in vivo.

74 ly proposed mechanism for energy coupling in lactose permease in which substrate binding causes a con

75 Site-directed chemical cleavage of lactose permease indicates that helix V is in close prox

76 MS-2 slides across TMS-7 and TMS-11 when the lactose permease interconverts between the C1 and C2 con

77 l Major Facilitator Superfamily transporter, lactose permease, into Droplet Interface Bilayers and de

78 ort a number of other lines of evidence that lactose permease is a monomer.

79 Lactose permease is a paradigm for the major facilitator

80 The lactose permease is an integral membrane protein that co

81 Lactose permease is an integral membrane protein that us

82 Specificity of substrate recognition in lactose permease is directed toward the galactosyl moiet

83 g of cyclohexyl alpha-D-galactopyranoside to lactose permease is essentially unchanged (K(D) = 0.4 mM

84 viding further support for the argument that lactose permease is functionally, as well as structurall

85 surface of enzyme IIAglc that interacts with lactose permease is proposed.

86 permease of Escherichia coli indicates that lactose permease is protonated prior to ligand binding.

87 he novel purification method described here, lactose permease is purified from beta-dodecyl maltoside

88 In this paper, 4B1 binding to purified lactose permease is shown to exhibit a KD of about 5 x 1

89 roposed that the central cytoplasmic loop of lactose permease is the major determinant for interactio

90 s study concerning the loop 2-3 motif of the lactose permease, it was shown that the first-position g

91 In lactose permease (lac permease), the most studied member

92 Lactose permease lacking epitope 4B1 can be induced to f

93 sing a model membrane protein (the bacterial lactose permease LacY reconstituted in proteoliposomes)

94 hermodynamics of ligand binding to wild-type lactose permease (LacY) and a mutant (C154G) that strong

95 coli (CscB) with the X-ray crystal structure lactose permease (LacY) as template reveals a similar ov

96 The lactose permease (LacY) catalyzes coupled stoichiometric

97 The lactose permease (LacY) catalyzes galactoside/H(+) sympo

98 six-helix bundles on the periplasmic side of lactose permease (LacY) cause complete loss of transport

99 t affinity (K(d)(app)) of purified wild-type lactose permease (LacY) for sugars was studied.

100 The N- and C-terminal six-helix bundles of lactose permease (LacY) form a large internal cavity ope

101 we describe an x-ray structure of wild-type lactose permease (LacY) from Escherichia coli determined

102 ny aspects of the fucose permease (FucP) and lactose permease (LacY) have also been investigated, whi

103 According to x-ray structure, the lactose permease (LacY) is a monomer organized into N- a

104 omain (C6) of the polytopic membrane protein lactose permease (LacY) is exposed to the opposite side

105 not energy-independent downhill transport by lactose permease (LacY) is impaired when expressed in Es

106 The N-terminal half of Escherichia coli lactose permease (LacY) is inverted with respect to the

107 The lactose permease (LacY) of Escherichia coli catalyzes st

108 wo novel ligand-free X-ray structures of the lactose permease (LacY) of Escherichia coli determined a

109 In vivo lactose permease (LacY) of Escherichia coli displays a m

110 Lactose permease (LacY) of Escherichia coli is an archet

111 The lactose permease (LacY) of Escherichia coli, a paradigm

112 established crystallization protocol for the lactose permease (LacY) of Escherichia coli, a systemati

113 Lactose permease (LacY) of Escherichia coli, when recons

114 he folding of the polytopic membrane protein lactose permease (LacY) of Escherichia coli.

115 Based on the crystal structure of lactose permease (LacY) open to the cytoplasm, a hybrid

116 olding in the lipid-dependent epitope 4B1 of lactose permease (LacY) resulting from in vivo assembly

117 X-ray crystal structures of lactose permease (LacY) reveal pseudosymmetrically arran

118 to the membrane bilayer of Escherichia coli lactose permease (LacY) transmembrane (TM) domains and t

119 Sugar/H(+) symport by lactose permease (LacY) utilizes an alternating access m

120 brane proteins, the function and assembly of lactose permease (LacY) was studied in mutants of Escher

121 The x-ray structure of the lactose permease (LacY) with bound substrate is consiste

122 Here, we use as a model the lactose permease (LacY), a membrane transport protein wi

123 Lactose permease (LacY), a paradigm for the largest fami

124 Lactose permease (LacY), a paradigm for the largest fami

125 rast to previous observations in the E. coli lactose permease (LacY), where most insertions in extram

126 membrane of Escherichia coli is catalyzed by lactose permease (LacY), which uses an alternating acces

127 ase (FucP) results in remarkable homology to lactose permease (LacY).

128 ary structure in the transmembrane domain of lactose permease (LacY).

129 glycerol-3-phosphate transporter (GlpT) and lactose permease (LacY).

130 yme IIAglc, indicating that these regions of lactose permease may be involved in recognition of enzym

131 inding, suggesting that sugar recognition in lactose permease may have evolved to discriminate primar

132 ry of the 12-helix bundle that comprises the lactose permease molecule.

133 Using a functional lactose permease mutant devoid of Cys residues (C-less p

134 Using a functional lactose permease mutant devoid of Cys residues (C-less p

135 Using a functional lactose permease mutant devoid of Cys residues (C-less p

136 Trp in transmembrane helix X of a functional lactose permease mutant devoid of Trp residues (Trp-less

137 In a functional lactose permease mutant from Escherichia coli (LacY) dev

138 Functional lactose permease mutants containing single Cys residues

139 o determine surface-exposed positions in 250 lactose permease mutants containing single-Cys replaceme

140 Functional lactose permease mutants containing single-Cys residues

141 Lactose permease mutants with polyhistidine insertions i

142 threaded through a crystal structure of the lactose permease of E. coli (LacY), manually adjusted, a

143 of fusions to the topologically well-studied lactose permease of E. coli and demonstrated that topolo

144 Lactose permease of Escherichia coli (lac Y) offers an o

145 l as solvent accessibility, by utilizing the lactose permease of Escherichia coli (LacY) as a model.

146 The x-ray structure of lactose permease of Escherichia coli (LacY) exhibits a s

147 rokaryotic transport proteins similar to the lactose permease of Escherichia coli (LacY) have been id

148 The lactose permease of Escherichia coli (LacY) is a highly

149 The lactose permease of Escherichia coli (LacY) is a highly

150 ependent lines of evidence indicate that the lactose permease of Escherichia coli (LacY) is highly dy

151 WT lactose permease of Escherichia coli (LacY) reconstitute

152 A key to obtaining an X-ray structure of the lactose permease of Escherichia coli (LacY) was the use

153 Trp mutant (Gly46-->Trp/Gly262-->Trp) of the lactose permease of Escherichia coli (LacY) with a bound

154 Lactose permease of Escherichia coli (LacY) with a singl

155 in topogenesis, insertion and folding of the lactose permease of Escherichia coli (LacY), a 12-transm

156 The lactose permease of Escherichia coli (LacY), a highly dy

157 The lactose permease of Escherichia coli (LacY), a highly dy

158 determined for sugar-binding affinity to the lactose permease of Escherichia coli (LacY), indicating

159 rected alkylation of Cys replacements in the lactose permease of Escherichia coli (LacY), the reactiv

160 eterminants for substrate recognition by the lactose permease of Escherichia coli are at the interfac

161 ch are critical for substrate binding in the lactose permease of Escherichia coli are charge paired a

162 lu126 (helix IV) and Arg144 (helix V) in the lactose permease of Escherichia coli are critical for su

163 d function of the polytopic membrane protein lactose permease of Escherichia coli are dependent on th

164 The lactose permease of Escherichia coli catalyzes coupled t

165 Helices IV and V in the lactose permease of Escherichia coli contain the major d

166 Helix X in the lactose permease of Escherichia coli contains two residu

167 We previously established that lactose permease of Escherichia coli displays a mixture

168 d that glutamate-126 and arginine-144 in the lactose permease of Escherichia coli form an ion pair th

169 ted into the central cytoplasmic loop of the lactose permease of Escherichia coli generating a high-a

170 al approaches, a helix packing model for the lactose permease of Escherichia coli has been proposed i

171 n of biochemical and biophysical data on the lactose permease of Escherichia coli has culminated in a

172 a5) from the central cytoplasmic loop of the lactose permease of Escherichia coli has no significant

173 Previous work on the lactose permease of Escherichia coli has shown that muta

174 Previous work on the lactose permease of Escherichia coli has shown that muta

175 as previously shown that coexpression of the lactose permease of Escherichia coli in two contiguous f

176 ism proposed for lactose/H(+) symport by the lactose permease of Escherichia coli indicates that lact

177 Cys-scanning mutagenesis of helix II in the lactose permease of Escherichia coli indicates that one

178 Lactose/H(+) symport by lactose permease of Escherichia coli involves interactio

179 Lactose permease of Escherichia coli is a polytopic memb

180 he first periplasmic loop (loop I/II) in the lactose permease of Escherichia coli is in close proximi

181 led translocation of substrate and H+ by the lactose permease of Escherichia coli is proposed, based

182 inal six-transmembrane domain (TM) bundle of lactose permease of Escherichia coli is uniformly invert

183 istic model for lactose/H(+) symport via the lactose permease of Escherichia coli proposed recently i

184 directed and Cys-scanning mutagenesis of the lactose permease of Escherichia coli reveals that as few

185 hysical, and crystallographic studies on the lactose permease of Escherichia coli suggest that Arg-14

186 The lactose permease of Escherichia coli transports protons

187 The lactose permease of Escherichia coli was expressed in tw

188 odification of transmembrane helix IX in the lactose permease of Escherichia coli was studied in righ

189 gand or monoclonal antibody (mAb) 4B1 in the lactose permease of Escherichia coli were studied.

190 ains in the galactoside/H(+) symporter LacY (lactose permease of Escherichia coli) are irreplaceable

191 X-ray crystal structures of LacY (lactose permease of Escherichia coli) exhibit a large cy

192 results are discussed in relationship to the lactose permease of Escherichia coli, a membrane transpo

193 ly of transport proteins, which includes the lactose permease of Escherichia coli, contains a highly

194 terminal transmembrane helices (C(6)) in the lactose permease of Escherichia coli, each containing a

195 rminal six transmembrane helices (C6) of the lactose permease of Escherichia coli, each with a Cys re

196 In the lactose permease of Escherichia coli, transmembrane heli

197 al epitope on the periplasmic surface of the lactose permease of Escherichia coli, uncoupling lactose

198 44 in helices IV and V, respectively, in the lactose permease of Escherichia coli, which play an indi

199 a critical role in substrate binding in the lactose permease of Escherichia coli.

200 to approximate loop-helix boundaries in the lactose permease of Escherichia coli.

201 zed here to measure helix proximities in the lactose permease of Escherichia coli.

202 well studied membrane transport protein, the lactose permease of Escherichia coli.

203 effect of pH on ligand binding in wild-type lactose permease or mutants in the four residues-Glu-269

204 es VII and VIII in the tertiary structure of lactose permease, other methods for binding rare earth m

205 upports the conclusion that the monodisperse lactose permease preparation is 80% alpha-helical and st

206 nd to be located at several sites within the lactose permease (Pro-28 --> Ser, Leu, or Thr; Phe-29 --

207 ns in the cytoplasmic N and C termini of the lactose permease protein, LacY, and replacement of all c

208 We found that the lactose permease purified from Escherichia coli cells ex

209 acetate treatment of enzyme IIAglc, but not lactose permease, reduced the degree of interaction betw

210 A collection of lactose permease replacement mutants at Cys-148 showed,

211 uggest that binding of various substrates to lactose permease results in a collection of unique confo

212 single amino acid deletions in the loops of lactose permease retain activity, while mutants with sin

213 e transport characteristics of the wild-type lactose permease, single mutants in which Lys-319 was ch

214 Lactose permease structure is deemed consistent with a m

215 ositions in the transmembrane helices of the lactose permease suggest that only positions accessible

216 been applied to the remaining 45 residues in lactose permease that have not been mutagenized previous

217 cterized the area on the cytoplasmic face of lactose permease that interacts with enzyme IIAglc, usin

218 B11 binds to a conformational epitope in the lactose permease that is exposed on the cytoplasmic face

219 y constrained mutant of the Escherichia coli lactose permease (the LacY double-Trp mutant Gly-46-->Tr

220 Cys mutants in putative periplasmic loops in lactose permease, three mutants [Tyr101 --> Cys (loop II

221 central role in governing the ability of the lactose permease to couple the transport of H+ and lacto

222 e EF-hand in the central cytoplasmic loop of lactose permease to positions 179 or 169 at the center o

223 teriorhodopsin was co-reconstituted with the lactose permease to provide a light-triggered electroche

224 Binding specificity in lactose permease toward galactopyranosides is governed b

225 mease, as well as functionally reconstituted lactose permease, using spectroscopic techniques.

226 f enzyme IIAglc with the cytoplasmic face of lactose permease was explored.

227 Here, Escherichia coli lactose permease was used in a novel spectroscopic metho

228 on of enzyme IIAglc with membrane-associated lactose permease was used to characterize the binding re

229 replacement mutants in cytoplasmic loops of lactose permease were evaluated for their capacity to bi

230 conformationally sensitive epitope (4B1) of lactose permease were used to establish a novel role for

231 ial structural and mechanistic homology with lactose permease, which belongs to the same sequence-def

232 Lactose permease with Cys154 --> Gly (helix V) binds sub

233 Treatment of lactose permease with N-ethylmaleimide, which blocks lig

234 By monitoring fluorescently labeled lactose permease with single-molecule sensitivity, we in

235 r, these results suggest that interaction of lactose permease with substrate promotes a conformationa