Ligand-dependent conformational plasticity of the periplasmic histidine-binding protein HisJ. Involvement in transport specificity (Q46687971)

24 December 2017

title

Ligand-dependent conformational plasticity of the periplasmic histidine-binding protein HisJ. Involvement in transport specificity (English)

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24 December 2017

author name string

Wolf A

1

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24 December 2017

Lee KC

2

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24 December 2017

Kirsch JF

3

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24 December 2017

Ames GF

4

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24 December 2017

language of work or name

English

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publication date

1 August 1996

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24 December 2017

Journal of Biological Chemistry

published in

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24 December 2017

volume

271

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24 December 2017

issue

35

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24 December 2017

page(s)

21243-21250

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24 December 2017

ATP-dependent transport systems in bacteria and humans: relevance to cystic fibrosis and multidrug resistance

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Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis

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The structural basis of sequence-independent peptide binding by OppA protein

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2 A resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor

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Crystal structure of the dipeptide binding protein from Escherichia coli involved in active transport and chemotaxis

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Fluorine-19 NMR studies of the D-galactose chemosensory receptor. 1. Sugar binding yields a global structural change

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Structure/function analysis of the periplasmic histidine-binding protein. Mutations decreasing ligand binding alter the properties of the conformational change and of the closed form

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C alpha-based torsion angles: a simple tool to analyze protein conformational changes

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Large amplitude twisting motions of an interdomain hinge: a disulfide trapping study of the galactose-glucose binding protein

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Substrate specificity and affinity of a protein modulated by bound water molecules

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Crystallographic analysis of the epimeric and anomeric specificity of the periplasmic transport/chemosensory protein receptor for D-glucose and D-galactose

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Liganded and unliganded receptors interact with equal affinity with the membrane complex of periplasmic permeases, a subfamily of traffic ATPases

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Quantitative assay of the binding of small molecules to protein: Comparison of dialysis and membrane filter assays

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Two periplasmic transport proteins which interact with a common membrane receptor show extensive homology: complete nucleotide sequences

21 January 2018

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Refined 1.89-A structure of the histidine-binding protein complexed with histidine and its relationship with many other active transport/chemosensory proteins

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A mutational hot-spot in the hisM gene of the histidine transport operon in Salmonella typhimurium is due to deletion of repeated sequences and results in an altered specificity of transport

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Genetic analysis of periplasmic binding protein dependent transport in Escherichia coli. Each lobe of maltose-binding protein interacts with a different subunit of the MalFGK2 membrane transport complex.

21 January 2018

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The ligand-binding domain in metabotropic glutamate receptors is related to bacterial periplasmic binding proteins

21 January 2018

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Agonist selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid-binding proteins

21 January 2018

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Glutamate receptor antibodies activate a subset of receptors and reveal an agonist binding site

21 January 2018

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Cloning and characterization of an extracellular Ca(2+)-sensing receptor from bovine parathyroid

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.271.35.21243

1 reference

24 December 2017

1 reference

24 December 2017