Structural Analysis of a Periplasmic Binding Protein in the Tripartite ATP-independent Transporter Family Reveals a Tetrameric Assembly That May Have a Role in Ligand Transport - Wikidata - wikimedia - TriplyDB

Structural Analysis of a Periplasmic Binding Protein in the Tripartite ATP-independent Transporter Family Reveals a Tetrameric Assembly That May Have a Role in Ligand Transport

Structural Analysis of a Periplasmic Binding Protein in the Tripartite ATP-independent Transporter Family Reveals a Tetrameric Assembly That May Have a Role in Ligand Transport

http://www.wikidata.org/entity/Q27651778

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Structure of the Escherichia coli phosphonate binding protein PhnD and rationally optimized phosphonate biosensors Evidence for an ABC-Type Riboflavin Transporter System in Pathogenic Spirochetes Structural, Bioinformatic, and In Vivo Analyses of Two Treponema pallidum Lipoproteins Reveal a Unique TRAP Transporter Molecular details of ligand selectivity determinants in a promiscuous β-glucan periplasmic binding protein A loose domain swapping organization confers a remarkable stability to the dimeric structure of the arginine binding protein from Thermotoga maritima Structure and functional analysis of the siderophore periplasmic binding protein from the fuscachelin gene cluster of Thermobifida fusca Evolution of the class C GPCR Venus flytrap modules involved positive selected functional divergence Tripartite ATP-independent periplasmic (TRAP) transporters in bacteria and archaea.The Tp0684 (MglB-2) Lipoprotein of Treponema pallidum: A Glucose-Binding Protein with Divergent Topology.Periplasmic Binding Proteins in Thermophiles: Characterization and Potential Application of an Arginine-Binding Protein from Thermotoga maritima: A Brief Thermo-Story.Studies of conformational changes of an arginine-binding protein from Thermotoga maritima in the presence and absence of ligand via molecular dynamics simulations with the coarse-grained UNRES force field.Amino acid transport in thermophiles: characterization of an arginine-binding protein in Thermotoga maritima.Tripartite ATP-Independent Periplasmic (TRAP) Transporters and Tripartite Tricarboxylate Transporters (TTT): From Uptake to Pathogenicity.

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P2860

Structural Analysis of a Periplasmic Binding Protein in the Tripartite ATP-independent Transporter Family Reveals a Tetrameric Assembly That May Have a Role in Ligand Transport

http://www.wikidata.org/entity/Q27651778

description

2008 nî lūn-bûn

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2008 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Structural Analysis of a Perip ...... ave a Role in Ligand Transport

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Structural Analysis of a Perip ...... ave a Role in Ligand Transport

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Structural Analysis of a Perip ...... ave a Role in Ligand Transport

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Structural Analysis of a Perip ...... ave a Role in Ligand Transport

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Structural Analysis of a Perip ...... ave a Role in Ligand Transport

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Structural Analysis of a Perip ...... ave a Role in Ligand Transport

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Structural Analysis of a Perip ...... ave a Role in Ligand Transport

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Structural Analysis of a Perip ...... ave a Role in Ligand Transport

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Structural Analysis of a Perip ...... ave a Role in Ligand Transport

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Journal of Biological Chemistry

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Structural analysis of a perip ...... ave a role in ligand transport

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Aleksandr E Miklos

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Anita Changela

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Homme W Hellinga

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Joanna K Krueger

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Lorena S Beese

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P2860

Crystal structures of an Extracytoplasmic Solute Receptor from a TRAP transporter in its open and closed forms reveal a helix-swapped dimer requiring a cation for alpha-keto acid binding

Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima

Determination of domain structure of proteins from X-ray solution scattering

Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria

TRAP transporters: a new family of periplasmic solute transport systems encoded by the dctPQM genes of Rhodobacter capsulatus and by homologs in diverse gram-negative bacteria

Improved methods for building protein models in electron density maps and the location of errors in these models

PROCHECK: a program to check the stereochemical quality of protein structures

X-ray crystallographic structures of the Escherichia coli periplasmic protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin

Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding

Crystal structures of two Bordetella pertussis periplasmic receptors contribute to defining a novel pyroglutamic acid binding DctP subfamily

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32812-32820

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scholarly article

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4025767

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10.1074/JBC.M803595200

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47

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283

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Matthew J Cuneo

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2008-08-22T00:00:00Z

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18723845

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2583322

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