Ferrichrome transport in Escherichia coli K-12: altered substrate specificity of mutated periplasmic FhuD and interaction of FhuD with the integral membrane protein FhuB.
about
Siderophore-based iron acquisition and pathogen controlCrystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuAX-ray crystallographic structures of the Escherichia coli periplasmic protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycinThe Staphylococcus aureus Siderophore Receptor HtsA Undergoes Localized Conformational Changes to Enclose Staphyloferrin A in an Arginine-rich Binding PocketStructures of Streptococcus pneumoniae PiaA and Its Complex with Ferrichrome Reveal Insights into the Substrate Binding and Release of High Affinity Iron TransportersStructural and functional characterization of the Staphylococcus aureus virulence factor and vaccine candidate FhuD2An update on the transport and metabolism of iron in Listeria monocytogenes: the role of proteins involved in pathogenicityIdentification of the periplasmic cobalamin-binding protein BtuF of Escherichia coli.The solution structure, binding properties, and dynamics of the bacterial siderophore-binding protein FepBIron starvation of Bordetella avium stimulates expression of five outer membrane proteins and regulates a gene involved in acquiring iron from serum.Interactions between TonB from Escherichia coli and the periplasmic protein FhuD.Binding of ferric enterobactin by the Escherichia coli periplasmic protein FepBBordetella pertussis FbpA binds both unchelated iron and iron siderophore complexes.A distinct mechanism for the ABC transporter BtuCD-BtuF revealed by the dynamics of complex formationSpecificity of Staphyloferrin B recognition by the SirA receptor from Staphylococcus aureus.FhuD1, a ferric hydroxamate-binding lipoprotein in Staphylococcus aureus: a case of gene duplication and lateral transfer.Microbial iron acquisition: marine and terrestrial siderophores.Mycobacteria, metals, and the macrophageUranium extremophily is an adaptive, rather than intrinsic, feature for extremely thermoacidophilic Metallosphaera speciesTwo molybdate/tungstate ABC transporters that interact very differently with their substrate binding proteins.Supramolecular interactions between functional metal complexes and proteins.Bacterial ATP-driven transporters of transition metals: physiological roles, mechanisms of action, and roles in bacterial virulence.Albomycin uptake via a ferric hydroxamate transport system of Streptococcus pneumoniae R6.The ABC maltose 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.ATP binding and hydrolysis disrupt the high-affinity interaction between the heme ABC transporter HmuUV and its cognate substrate-binding protein.Sideromycins: tools and antibioticsDocking of the periplasmic FecB binding protein to the FecCD transmembrane proteins in the ferric citrate transport system of Escherichia coliUptake of xenosiderophores in Bacillus subtilis occurs with high affinity and enhances the folding stabilities of substrate binding proteins.The role of FhuD2 in iron(III)-hydroxamate transport in Staphylococcus aureus. Demonstration that FhuD2 binds iron(III)-hydroxamates but with minimal conformational change and implication of mutations on transport.Isolation and structural identification of the trihydroxamate siderophore vicibactin and its degradative products from Rhizobium leguminosarum ATCC 14479 bv. trifolii.
P2860
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P2860
Ferrichrome transport in Escherichia coli K-12: altered substrate specificity of mutated periplasmic FhuD and interaction of FhuD with the integral membrane protein FhuB.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
Ferrichrome transport in Esche ...... ntegral membrane protein FhuB.
@en
Ferrichrome transport in Esche ...... ntegral membrane protein FhuB.
@nl
type
label
Ferrichrome transport in Esche ...... ntegral membrane protein FhuB.
@en
Ferrichrome transport in Esche ...... ntegral membrane protein FhuB.
@nl
prefLabel
Ferrichrome transport in Esche ...... ntegral membrane protein FhuB.
@en
Ferrichrome transport in Esche ...... ntegral membrane protein FhuB.
@nl
P2093
P2860
P1476
Ferrichrome transport in Esche ...... ntegral membrane protein FhuB.
@en
P2093
P2860
P304
P356
10.1128/JB.177.24.7186-7193.1995
P577
1995-12-01T00:00:00Z