ライフサイエンスコーパス: lactose permease

1 s major facilitator transporter superfamily, lactose permease.

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

3 erase system inhibits transport catalyzed by lactose permease.

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

5 9 were mutagenized and tested for binding to lactose permease.

6 urface of enzyme IIAglc that interfaces with lactose permease.

7 and on proteoliposomes containing functional lactose permease.

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

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

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

11 at a step corresponding to deprotonation of lactose permease.

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

13 a molecular hinge between the two halves of 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 The lactose permease is an integral membrane protein that co

80 Lactose permease is an integral membrane protein that us

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

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

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

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

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

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

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

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

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

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

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

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

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

94 The lactose permease (LacY) catalyzes coupled stoichiometric

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

135 Functional lactose permease mutants containing single Cys residues

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

137 Functional lactose permease mutants containing single-Cys residues

138 Lactose permease mutants with polyhistidine insertions i

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

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

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

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

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

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

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

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

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

148 WT lactose permease of Escherichia coli (LacY) reconstitute

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

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

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

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

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

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

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

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

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

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

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

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

161 The lactose permease of Escherichia coli catalyzes coupled t

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

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

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

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

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

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

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

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

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

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

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

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

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

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

176 Lactose permease of Escherichia coli is a polytopic memb

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

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

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

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

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

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

183 The lactose permease of Escherichia coli transports protons

184 The lactose permease of Escherichia coli was expressed in tw

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

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

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

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

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

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

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

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

193 In the lactose permease of Escherichia coli, transmembrane heli

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

195 44 in helices IV and V, respectively, in the lactose permease of Escherichia coli, which play an indi

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

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

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

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

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

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

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

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

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

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

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

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

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

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

210 Lactose permease structure is deemed consistent with a m

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

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

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

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

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

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

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

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

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

220 Binding specificity in lactose permease toward galactopyranosides is governed b

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

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

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

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

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

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

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

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

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

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

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