A structural and functional analysis of type III periplasmic and substrate binding proteins: their role in bacterial siderophore and heme transport.
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Solution Structure of Escherichia coli FeoA and Its Potential Role in Bacterial Ferrous Iron TransportEvidence for an allosteric mechanism of substrate release from membrane-transporter accessory binding proteinsRole of the Two Structural Domains from the Periplasmic Escherichia coli Histidine-binding Protein HisJInteractions of a periplasmic binding protein with a tetradentate siderophore mimicStructure and functional analysis of the siderophore periplasmic binding protein from the fuscachelin gene cluster of Thermobifida fuscaLipoprotein FtsB in Streptococcus pyogenes binds ferrichrome in two steps with residues Tyr137 and Trp204 as critical ligandsMolecular dynamics simulations reveal that apo-HisJ can sample a closed conformation.The solution structure, binding properties, and dynamics of the bacterial siderophore-binding protein FepBBordetella pertussis FbpA binds both unchelated iron and iron siderophore complexes.Apo, Zn2+-bound and Mn2+-bound structures reveal ligand-binding properties of SitA from the pathogen Staphylococcus pseudintermedius.Possible role of Escherichia coli in propagation and perpetuation of chronic inflammation in ulcerative colitisThe dual role of Escherichia coli in the course of ulcerative colitis.Vibrio Iron Transport: Evolutionary Adaptation to Life in Multiple Environments.Heme Binding by Corynebacterium diphtheriae HmuT: Function and Heme Environment.Heme-bound SiaA from Streptococcus pyogenes: Effects of mutations and oxidation state on protein stability.Quantitative proteomic analysis of cell envelope preparations under iron starvation stress in Aeromonas hydrophila.Protein conformational switches: from nature to design.Recent developments in understanding the iron acquisition strategies of gram positive pathogens.Ligand binding specificity of the Escherichia coli periplasmic histidine binding protein, HisJ.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.Crystal structure of FhuD at 1.6 Å resolution: a ferrichrome-binding protein from the animal and human pathogen Staphylococcus pseudintermedius.Structure and dynamics of Type III periplasmic proteins VcFhuD and VcHutB reveal molecular basis of their distinctive ligand binding properties.Escherichia [corrected] coli ribose binding protein based bioreporters revisited.Uptake of xenosiderophores in Bacillus subtilis occurs with high affinity and enhances the folding stabilities of substrate binding proteins.
P2860
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P2860
A structural and functional analysis of type III periplasmic and substrate binding proteins: their role in bacterial siderophore and heme transport.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on January 2011
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
A structural and functional an ...... iderophore and heme transport.
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A structural and functional an ...... iderophore and heme transport.
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type
label
A structural and functional an ...... iderophore and heme transport.
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A structural and functional an ...... iderophore and heme transport.
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prefLabel
A structural and functional an ...... iderophore and heme transport.
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A structural and functional an ...... iderophore and heme transport.
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P2860
P356
P1433
P1476
A structural and functional an ...... iderophore and heme transport.
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P2093
Byron C H Chu
Hans J Vogel
P2860
P356
10.1515/BC.2011.012
P577
2011-01-01T00:00:00Z