Literature DB >> 9573164

Suppressor scanning at positions 177 and 236 in the Escherichia coli lactose/H+ cotransporter and stereotypical effects of acidic substituents that suggest a favored orientation of transmembrane segments relative to the lipid bilayer.

S C King1, S Li.   

Abstract

Acidic substituents for Ala-177 (helix 6) or Tyr-236 (helix 7) in LacY cause effects on sugar recognition and cosubstrate coupling that are stereotypical of neutral substituents. Thus, helices 6 and 7 are probably oriented to produce little side-chain contact with the low dielectric lipid bilayer at positions 177 and 236.

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Year:  1998        PMID： 9573164      PMCID： PMC107231          DOI： 10.1128/JB.180.10.2756-2758.1998

Source DB:  PubMed          Journal:  J Bacteriol        ISSN： 0021-9193            Impact factor:   3.490


  16 in total

Review 1.  Electrostatic interactions in membranes and proteins.

Authors:  B H Honig; W L Hubbell; R F Flewelling
Journal:  Annu Rev Biophys Biophys Chem       Date:  1986

Review 2.  Towards an understanding of the structural basis of 'forbidden' transport pathways in the Escherichia coli lactose carrier: mutations probing the energy barriers to uncoupled transport.

Authors:  S C King; T H Wilson
Journal:  Mol Microbiol       Date:  1990-09       Impact factor: 3.501

3.  An analysis of suppressor mutations suggests that the two halves of the lactose permease function in a symmetrical manner.

Authors:  N J Pazdernik; S M Cain; R J Brooker
Journal:  J Biol Chem       Date:  1997-10-17       Impact factor: 5.157

4.  Sensitivity of efflux-driven carrier turnover to external pH in mutants of the Escherichia coli lactose carrier that have tyrosine or phenylalanine substituted for histidine-322. A comparison of lactose and melibiose.

Authors:  S C King; T H Wilson
Journal:  J Biol Chem       Date:  1990-02-25       Impact factor: 5.157

5.  Identification of valine 177 as a mutation altering specificity for transport of sugars by the Escherichia coli lactose carrier. Enhanced specificity for sucrose and maltose.

Authors:  S C King; T H Wilson
Journal:  J Biol Chem       Date:  1990-06-15       Impact factor: 5.157

6.  Characterization of Escherichia coli lactose carrier mutants that transport protons without a cosubstrate. Probes for the energy barrier to uncoupled transport.

Authors:  S C King; T H Wilson
Journal:  J Biol Chem       Date:  1990-06-15       Impact factor: 5.157

7.  Galactoside-dependent proton transport by mutants of the Escherichia coli lactose carrier. Replacement of histidine 322 by tyrosine or phenylalanine.

Authors:  S C King; T H Wilson
Journal:  J Biol Chem       Date:  1989-05-05       Impact factor: 5.157

8.  lac permease of Escherichia coli: histidine-322 and glutamic acid-325 may be components of a charge-relay system.

Authors:  N Carrasco; L M Antes; M S Poonian; H R Kaback
Journal:  Biochemistry       Date:  1986-08-12       Impact factor: 3.162

9.  An analysis of lactose permease "sugar specificity" mutations which also affect the coupling between proton and lactose transport. I. Val177 and Val177/Asn319 permeases facilitate proton uniport and sugar uniport.

Authors:  R J Brooker
Journal:  J Biol Chem       Date:  1991-03-05       Impact factor: 5.157

10.  Characterization of site-directed mutants in the lac permease of Escherichia coli. 1. Replacement of histidine residues.

Authors:  I B Püttner; H K Sarkar; E Padan; J S Lolkema; H R Kaback
Journal:  Biochemistry       Date:  1989-03-21       Impact factor: 3.162
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  2 in total

1.  Evidence for the transport of maltose by the sucrose permease, CscB, of Escherichia coli.

Authors:  Yang Peng; Sanath Kumar; Ricardo L Hernandez; Suzanna E Jones; Kathleen M Cadle; Kenneth P Smith; Manuel F Varela
Journal:  J Membr Biol       Date:  2009-03-18       Impact factor: 1.843

2.  Functional characterization of cysteine residues in GlpT, the glycerol 3-phosphate transporter of Escherichia coli.

Authors:  Mon-Chou Fann; Anne Busch; Peter C Maloney
Journal:  J Bacteriol       Date:  2003-07       Impact factor: 3.490
  2 in total

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