Holo- and apo-bound structures of bacterial periplasmic heme-binding proteins - Wikidata - wikimedia - TriplyDB

Holo- and apo-bound structures of bacterial periplasmic heme-binding proteins

Holo- and apo-bound structures of bacterial periplasmic heme-binding proteins

http://www.wikidata.org/entity/Q27648739

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Product Release Rather than Chelation Determines Metal Specificity for Ferrochelatase Characterization of a Bacillus subtilis transporter for petrobactin, an anthrax stealth siderophore The Staphylococcus aureus Siderophore Receptor HtsA Undergoes Localized Conformational Changes to Enclose Staphyloferrin A in an Arginine-rich Binding Pocket Discovery and characterization of a unique mycobacterial heme acquisition system Crystal structure of the Pseudomonas aeruginosa cytoplasmic heme binding protein, Apo-PhuS Replacing the Axial Ligand Tyrosine 75 or Its Hydrogen Bond Partner Histidine 83 Minimally Affects Hemin Acquisition by the Hemophore HasAp from Pseudomonas aeruginosa Helicobacter pylori periplasmic receptor CeuE (HP1561) modulates its nickel affinity via organic metallophores Structure and functional analysis of the siderophore periplasmic binding protein from the fuscachelin gene cluster of Thermobifida fusca The solution structure, binding properties, and dynamics of the bacterial siderophore-binding protein FepB Mapping ultra-weak protein-protein interactions between heme transporters of Staphylococcus aureus A distinct mechanism for the ABC transporter BtuCD-BtuF revealed by the dynamics of complex formation Induced fit on heme binding to the Pseudomonas aeruginosa cytoplasmic protein (PhuS) drives interaction with heme oxygenase (HemO)Specificity of Staphyloferrin B recognition by the SirA receptor from Staphylococcus aureus.Differential contributions of the outer membrane receptors PhuR and HasR to heme acquisition in Pseudomonas aeruginosa.Characterization of heme ligation properties of Rv0203, a secreted heme binding protein involved in Mycobacterium tuberculosis heme uptake.Structural Characterization of Heme Environmental Mutants of CgHmuT that Shuttles Heme Molecules to Heme Transporters Heme Binding by Corynebacterium diphtheriae HmuT: Function and Heme Environment.Bacterial heme-transport proteins and their heme-coordination modes.Role and regulation of heme iron acquisition in gram-negative pathogens.Canonical and ECF-type ATP-binding cassette importers in prokaryotes: diversity in modular organization and cellular functions.A structural and functional analysis of type III periplasmic and substrate binding proteins: their role in bacterial siderophore and heme transport.Recent advances in bacterial heme protein biochemistry.Bacterial ATP-driven transporters of transition metals: physiological roles, mechanisms of action, and roles in bacterial virulence.Ligand binding specificity of the Escherichia coli periplasmic histidine binding protein, HisJ.Purification, crystallization and preliminary X-ray analysis of the periplasmic haem-binding protein HutB from Vibrio cholerae.Functional characterization of the Shigella dysenteriae heme ABC transporter.FecB, a periplasmic ferric-citrate transporter from E. coli, can bind different forms of ferric-citrate as well as a wide variety of metal-free and metal-loaded tricarboxylic acids.Spectroscopic Determination of Distinct Heme Ligands in Outer-Membrane Receptors PhuR and HasR of Pseudomonas aeruginosa.Spectroscopic and mutagenesis studies of human PGRMC1.Extracellular heme uptake and the challenges of bacterial cell membranes.Structure and dynamics of Type III periplasmic proteins VcFhuD and VcHutB reveal molecular basis of their distinctive ligand binding properties.Structural basis for binding and transfer of heme in bacterial heme-acquisition systems.Characterization of the second conserved domain in the heme uptake protein HtaA from Corynebacterium diphtheriae.Genome scale identification, structural analysis, and classification of periplasmic binding proteins from Mycobacterium tuberculosis.Corynebacterium diphtheriae HmuT: dissecting the roles of conserved residues in heme pocket stabilization.

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P2860

Holo- and apo-bound structures of bacterial periplasmic heme-binding proteins

http://www.wikidata.org/entity/Q27648739

description

2007 nî lūn-bûn

@nan

2007 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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name

Holo- and apo-bound structures of bacterial periplasmic heme-binding proteins

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Holo- and apo-bound structures of bacterial periplasmic heme-binding proteins

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Holo- and apo-bound structures of bacterial periplasmic heme-binding proteins

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type

label

Holo- and apo-bound structures of bacterial periplasmic heme-binding proteins

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Holo- and apo-bound structures of bacterial periplasmic heme-binding proteins

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Holo- and apo-bound structures of bacterial periplasmic heme-binding proteins

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prefLabel

Holo- and apo-bound structures of bacterial periplasmic heme-binding proteins

@ast

Holo- and apo-bound structures of bacterial periplasmic heme-binding proteins

@en

Holo- and apo-bound structures of bacterial periplasmic heme-binding proteins

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P1433

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Journal of Biological Chemistry

P1476

Holo- and apo-bound structures of bacterial periplasmic heme-binding proteins

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P2093

Angela Wilks

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Huiying Li

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Maolin Guo

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Suntara Eakanunkul

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Thomas L Poulos

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Winny W Ho

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Yong Tong

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P2860

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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

The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter

Oxo-iron clusters in a bacterial iron-trafficking protein: new roles for a conserved motif

ARP/wARP and molecular replacement

Methods used in the structure determination of bovine mitochondrial F1 ATPase

Solvent content of protein crystals

A graphical user interface to the CCP4 program suite

Solving structures of protein complexes by molecular replacement with Phaser

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scholarly article

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1237117

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10.1074/JBC.M706761200

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49

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282

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2007-12-07T00:00:00Z

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17925389

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