Functionally distinct NEAT (NEAr Transporter) domains within the Staphylococcus aureus IsdH/HarA protein extract heme from methemoglobin. - Test2 - elhamkhani - TriplyDB

Functionally distinct NEAT (NEAr Transporter) domains within the Staphylococcus aureus IsdH/HarA protein extract heme from methemoglobin.

Functionally distinct NEAT (NEAr Transporter) domains within the Staphylococcus aureus IsdH/HarA protein extract heme from methemoglobin.

http://www.wikidata.org/entity/Q30157469

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Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humans Haemophore functions revisited Unique Heme-Iron Coordination by the Hemoglobin Receptor IsdB of Staphylococcus aureus Structural Basis for Hemoglobin Capture by Staphylococcus aureus Cell-surface Protein, IsdH Staphylococcus aureus Uses a Novel Multidomain Receptor to Break Apart Human Hemoglobin and Steal Its Heme The Near-iron Transporter (NEAT) Domains of the Anthrax Hemophore IsdX2 Require a Critical Glutamine to Extract Heme from Methemoglobin Differential Function of Lip Residues in the Mechanism and Biology of an Anthrax Hemophore Structure of the Hemoglobin-IsdH Complex Reveals the Molecular Basis of Iron Capture byStaphylococcus aureus Solution Structure and Molecular Determinants of Hemoglobin Binding of the First NEAT Domain of IsdB in Staphylococcus aureus The structure of haemoglobin bound to the haemoglobin receptor IsdH from Staphylococcus aureus shows disruption of the native α-globin haem pocket Molecular and evolutionary analysis of NEAr-iron Transporter (NEAT) domains Molecular mechanisms of bio-catalysis of heme extraction from hemoglobin Heme transfer to the bacterial cell envelope occurs via a secreted hemophore in the Gram-positive pathogen Bacillus anthracis.Heme uptake in bacterial pathogens IsdB-dependent hemoglobin binding is required for acquisition of heme by Staphylococcus aureus.A Bacillus anthracis S-layer homology protein that binds heme and mediates heme delivery to IsdC The ABC transporter HrtAB confers resistance to hemin toxicity and is regulated in a hemin-dependent manner by the ChrAS two-component system in Corynebacterium diphtheriae.Molecular strategies of microbial iron assimilation: from high-affinity complexes to cofactor assembly systems.Novel mechanism of hemin capture by Hbp2, the hemoglobin-binding hemophore from Listeria monocytogenes.Utilization of host iron sources by Corynebacterium diphtheriae: multiple hemoglobin-binding proteins are essential for the use of iron from the hemoglobin-haptoglobin complex.IsdA and IsdB antibodies protect mice against Staphylococcus aureus abscess formation and lethal challenge Novel hemin binding domains in the Corynebacterium diphtheriae HtaA protein interact with hemoglobin and are critical for heme iron utilization by HtaA The five near-iron transporter (NEAT) domain anthrax hemophore, IsdX2, scavenges heme from hemoglobin and transfers heme to the surface protein IsdC.The PRE-Derived NMR Model of the 38.8-kDa Tri-Domain IsdH Protein from Staphylococcus aureus Suggests That It Adaptively Recognizes Human Hemoglobin.Protective efficacy of the chimeric Staphylococcus aureus vaccine candidate IC in sepsis and pneumonia models Backbone 1H, 13C and 15N resonance assignments of the 39 kDa staphylococcal hemoglobin receptor IsdH Analysis of novel iron-regulated, surface-anchored hemin-binding proteins in Corynebacterium diphtheriae ¹H, ¹³C, ¹⁵N backbone and side chain NMR resonance assignments of the N-terminal NEAr iron transporter domain 1 (NEAT 1) of the hemoglobin receptor IsdB of Staphylococcus aureus Molecular mechanisms of Staphylococcus aureus iron acquisition.Subcellular localization of the Staphylococcus aureus heme iron transport components IsdA and IsdB.Axial ligand replacement mechanism in heme transfer from streptococcal heme-binding protein Shp to HtsA of the HtsABC transporter Mechanisms of iron import in anthrax.Recent advances in bacterial heme protein biochemistry.The theft of host heme by Gram-positive pathogenic bacteria.Mechanisms of iron and haem transport by Listeria monocytogenes.Adhesion, invasion and evasion: the many functions of the surface proteins of Staphylococcus aureus.Recent developments in understanding the iron acquisition strategies of gram positive pathogens.Heme Synthesis and Acquisition in Bacterial Pathogens.The ClusPro web server for protein-protein docking.The Staphylococcus aureus Protein IsdH Inhibits Host Hemoglobin Scavenging to Promote Heme Acquisition by the Pathogen.

P2860

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P2860

Functionally distinct NEAT (NEAr Transporter) domains within the Staphylococcus aureus IsdH/HarA protein extract heme from methemoglobin.

http://www.wikidata.org/entity/Q30157469

description

2008 nî lūn-bûn

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2008 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2008 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2008年の論文

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Functionally distinct NEAT (NE ...... tract heme from methemoglobin.

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Functionally distinct NEAT (NE ...... tract heme from methemoglobin.

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Functionally distinct NEAT (NE ...... tract heme from methemoglobin.

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Functionally distinct NEAT (NE ...... tract heme from methemoglobin.

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Functionally distinct NEAT (NE ...... tract heme from methemoglobin.

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Journal of Biological Chemistry

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Functionally distinct NEAT (NE ...... tract heme from methemoglobin.

@en

P2093

Martin Phillips

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

Melissa L Wong

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

Robert T Clubb

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Rosemarie M Pilpa

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Scott A Robson

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Valerie A Villareal

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P2860

Crystal structure of the catalytic domain of human complement c1s: a serine protease with a handle

Covalent structure of human haptoglobin: a serine protease homolog

NEAT: a domain duplicated in genes near the components of a putative Fe3+ siderophore transporter from Gram-positive pathogenic bacteria.

Haem recognition by a Staphylococcus aureus NEAT domain

The IsdC Protein from Staphylococcus aureus Uses a Flexible Binding Pocket to Capture Heme

His64(E7)-->Tyr apomyoglobin as a reagent for measuring rates of hemin dissociation

The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling

Staphylococcus aureus infections

Bacterial iron homeostasis

High-affinity binding of the staphylococcal HarA protein to haptoglobin and hemoglobin involves a domain with an antiparallel eight-stranded beta-barrel fold.

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1166-1176

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10.1074/JBC.M806007200

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2

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284

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18984582

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2613621

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