Heme uptake across the outer membrane as revealed by crystal structures of the receptor-hemophore complex - Wikidata - awgldk - TriplyDB

Heme uptake across the outer membrane as revealed by crystal structures of the receptor-hemophore complex

Heme uptake across the outer membrane as revealed by crystal structures of the receptor-hemophore complex

http://www.wikidata.org/entity/Q27653432

about

Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humans The structural biology of β-barrel membrane proteins: a summary of recent reports Haemophore functions revisited Beware of proteins bearing gifts: protein antibiotics that use iron as a Trojan horse Rapid Heme Transfer Reactions between NEAr Transporter Domains of Staphylococcus aureus: A Theoretical Study Using QM/MM and MD Simulations Unique Structure and Stability of HmuY, a Novel Heme-Binding Protein of Porphyromonas gingivalis Structural, NMR Spectroscopic, and Computational Investigation of Hemin Loading in the Hemophore HasAp from Pseudomonas aeruginosa Use of a molecular decoy to segregate transport from antigenicity in the FrpB iron transporter from Neisseria meningitidis The Structure of HasB Reveals a New Class of TonB Protein Fold The Hemophore HasA from Yersinia pestis (HasA yp ) Coordinates Hemin with a Single Residue, Tyr75, and with Minimal Conformational Change Interaction of a Partially Disordered Antisigma Factor with Its Partner, the Signaling Domain of the TonB-Dependent Transporter HasR X-ray structure of the Yersinia pestis heme transporter HmuUV Structure of the bacterial plant-ferredoxin receptor FusA Metabolic flux of extracellular heme uptake in Pseudomonas aeruginosa is driven by the iron-regulated heme oxygenase (HemO)Continuous Reusability using Immobilized HasApf in Chemoenzymatic Deracemization: A New Heterogeneous Enzyme Catalysis Structural basis of the signalling through a bacterial membrane receptor HasR deciphered by an integrative approach Ser/Thr motifs in transmembrane proteins: conservation patterns and effects on local protein structure and dynamics Structures of membrane proteins.Heme transfer to the bacterial cell envelope occurs via a secreted hemophore in the Gram-positive pathogen Bacillus anthracis.Kinetic and spectroscopic studies of hemin acquisition in the hemophore HasAp from Pseudomonas aeruginosa.TonB-dependent transporters: regulation, structure, and function.Induced fit on heme binding to the Pseudomonas aeruginosa cytoplasmic protein (PhuS) drives interaction with heme oxygenase (HemO)Role of the iron axial ligands of heme carrier HasA in heme uptake and release.Characterization of a hemophore-like protein from Porphyromonas gingivalis.Variation and molecular evolution of HmbR, the Neisseria meningitidis haemoglobin receptor New insights into iron acquisition by cyanobacteria: an essential role for ExbB-ExbD complex in inorganic iron uptake Microbial iron acquisition: marine and terrestrial siderophores.Differential contributions of the outer membrane receptors PhuR and HasR to heme acquisition in Pseudomonas aeruginosa.Transient weak protein-protein complexes transfer heme across the cell wall of Staphylococcus aureus.Spectroscopic evidence for a 5-coordinate oxygenic ligated high spin ferric heme moiety in the Neisseria meningitidis hemoglobin binding receptor.Refolding, purification and crystallization of the FrpB outer membrane iron transporter from Neisseria meningitidis Mycobacteria, metals, and the macrophage The molecular mechanism of Zinc acquisition by the neisserial outer-membrane transporter ZnuD.PPE Surface Proteins Are Required for Heme Utilization by Mycobacterium tuberculosis.Mechanistic Implications of the Unique Structural Features and Dimerization of the Cytoplasmic Domain of the Pseudomonas Sigma Regulator, PupR The P. aeruginosa heme binding protein PhuS is a heme oxygenase titratable regulator of heme uptake Sequestration and scavenging of iron in infection.Axial ligand replacement mechanism in heme transfer from streptococcal heme-binding protein Shp to HtsA of the HtsABC transporter Surf1, associated with Leigh syndrome in humans, is a heme-binding protein in bacterial oxidase biogenesis Trafficking of heme and porphyrins in metazoa.

P2860

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P2860

Heme uptake across the outer membrane as revealed by crystal structures of the receptor-hemophore complex

http://www.wikidata.org/entity/Q27653432

description

2009 nî lūn-bûn

@nan

2009 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հունվարին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

@zh-hk

2009年論文

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2009年論文

@zh-tw

2009年论文

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name

Heme uptake across the outer m ...... the receptor-hemophore complex

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Heme uptake across the outer m ...... the receptor-hemophore complex

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Heme uptake across the outer m ...... the receptor-hemophore complex

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type

label

Heme uptake across the outer m ...... the receptor-hemophore complex

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Heme uptake across the outer m ...... the receptor-hemophore complex

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Heme uptake across the outer m ...... the receptor-hemophore complex

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prefLabel

Heme uptake across the outer m ...... the receptor-hemophore complex

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Heme uptake across the outer m ...... the receptor-hemophore complex

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Heme uptake across the outer m ...... the receptor-hemophore complex

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PNAS.0809406106

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Proceedings of the National Academy of Sciences of the United States of America

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Heme uptake across the outer m ...... the receptor-hemophore complex

@en

P2093

Anne Lecroisey

http://www.w3.org/2001/XMLSchema#string

Cécile Wandersman

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Frédéric Huché

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Nadia Izadi-Pruneyre

http://www.w3.org/2001/XMLSchema#string

Philippe Delepelaire

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Stefanie Krieg

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P2860

The Protein Data Bank

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

A short history of SHELX

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

The crystal structure of HasA, a hemophore secreted by Serratia marcescens

Structural basis of gating by the outer membrane transporter FecA

Substrate-induced transmembrane signaling in the cobalamin transporter BtuB

Crystal structure of a catalytic intermediate of the maltose transporter

Comparative analysis of structural and dynamic properties of the loaded and unloaded hemophore HasA: functional implications

Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide

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1045-50

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1569640

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10.1073/PNAS.0809406106

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4

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106

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2009-01-27T00:00:00Z

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41519961

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19144921

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crystal structure

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2633585

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