Thermodynamics and dynamics of histidine-binding protein, the water-soluble receptor of histidine permease. Implications for the transport of high and low affinity ligands (Q41743298)

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scientific article published on July 2000

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English	Thermodynamics and dynamics of histidine-binding protein, the water-soluble receptor of histidine permease. Implications for the transport of high and low affinity ligands	scientific article published on July 2000

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

8 October 2017

Thermodynamics and dynamics of histidine-binding protein, the water-soluble receptor of histidine permease. Implications for the transport of high and low affinity ligands (English)

1 reference

Europe PubMed Central

PubMed publication ID

8 October 2017

author name string

D I Kreimer

1

1 reference

Europe PubMed Central

PubMed publication ID

8 October 2017

H Malak

2

1 reference

Europe PubMed Central

PubMed publication ID

8 October 2017

J R Lakowicz

3

1 reference

Europe PubMed Central

PubMed publication ID

8 October 2017

S Trakhanov

4

1 reference

Europe PubMed Central

PubMed publication ID

8 October 2017

E Villar

5

1 reference

Europe PubMed Central

PubMed publication ID

8 October 2017

V L Shnyrov

6

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Europe PubMed Central

PubMed publication ID

8 October 2017

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publication date

1 July 2000

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Europe PubMed Central

PubMed publication ID

8 October 2017

1 reference

Europe PubMed Central

PubMed publication ID

8 October 2017

267

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Europe PubMed Central

PubMed publication ID

8 October 2017

13

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Europe PubMed Central

PubMed publication ID

8 October 2017

4242-4252

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Europe PubMed Central

PubMed publication ID

8 October 2017

Structural mechanisms for domain movements in proteins

1 reference

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Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes

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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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Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor

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Perturbation of the equilibrium between open and closed conformations of the periplasmic C4-dicarboxylate binding protein from Rhodobacter capsulatus

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

1 reference

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Two modes of ligand binding in maltose-binding protein of Escherichia coli. Electron paramagnetic resonance study of ligand-induced global conformational changes by site-directed spin labeling

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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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Fluorine-19 nuclear magnetic resonance study of 5-fluorotryptophan-labeled histidine-binding protein J of Salmonella typhimurium

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Conformational changes of three periplasmic receptors for bacterial chemotaxis and transport: the maltose-, glucose/galactose- and ribose-binding proteins.

1 reference

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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

1 reference

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1 reference

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Thermodynamic characterization of the reversible, two-state unfolding of maltose binding protein, a large two-domain protein

1 reference

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21 January 2018

Thermodynamics of maltose binding protein unfolding

1 reference

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Peptide Binding in OppA, the Crystal Structures of the Periplasmic Oligopeptide Binding Protein in the Unliganded Form and in Complex with Lysyllysine,

1 reference

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Bacterial periplasmic transport systems: structure, mechanism, and evolution

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

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

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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

1 reference

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21 January 2018

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

1 reference

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Two partially unfolded states of Torpedo californica acetylcholinesterase

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Distance-dependent fluorescence quenching of tryptophan by acrylamide.

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Aromatic Contributions To Circular Dichroism Spectra Of Protein

1 reference

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Circular dichroism

1 reference

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Crystallization and preliminary X-ray crystallographic data of a histidine-binding protein from Escherichia coli

1 reference

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Nucleotide sequence of the partition locus of Escherichia coli plasmid pSC101

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Both lobes of the soluble receptor of the periplasmic histidine permease, an ABC transporter (traffic ATPase), interact with the membrane-bound complex. Effect of different ligands and consequences for the mechanism of action

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Some factors in the interpretation of protein denaturation

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Thermodynamics of the temperature‐induced unfolding of globular proteins

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Binding in the growth hormone receptor complex

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The 1.7 A refined X-ray structure of the periplasmic glucose/galactose receptor from Salmonella typhimurium

1 reference

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Substitution of a proline for alanine 183 in the hinge region of phosphoglycerate kinase: effects on catalysis, activation by sulfate, and thermal stability

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A simple model for proteins with interacting domains. Applications to scanning calorimetry data

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CHAIN: a crystallographic modeling program

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Identifiers

10.1046/J.1432-1033.2000.01470.X

1 reference

Europe PubMed Central

PubMed publication ID

8 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

8 October 2017

ResearchGate publication ID

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