Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone
about
Structure, function, and evolution of bacterial ATP-binding cassette systemsDiversity in coding tandem repeats in related Neisseria sppManganese and microbial pathogenesis: sequestration by the Mammalian immune system and utilization by microorganismsThe crystal structure of Zn(II)-free Treponema pallidum TroA, a periplasmic metal-binding protein, reveals a closed conformation.Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand bindingThe structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporterCrystal structures of the liganded and unliganded nickel-binding protein NikA from Escherichia coliCrystal structure of the Tp34 (TP0971) lipoprotein of treponema pallidum: implications of its metal-bound state and affinity for human lactoferrinStructural Analysis of ABC-family Periplasmic Zinc Binding Protein Provides New Insights Into Mechanism of Ligand Uptake and ReleaseThe Laminin-Binding Protein Lbp from Streptococcus pyogenes Is a Zinc ReceptorHeme coordination by Staphylococcus aureus IsdEThe solution structure of the periplasmic domain of the TonB system ExbD protein reveals an unexpected structural homology with siderophore-binding proteinsStructure and metal binding properties of ZnuA, a periplasmic zinc transporter from Escherichia coliThe Staphylococcus aureus Siderophore Receptor HtsA Undergoes Localized Conformational Changes to Enclose Staphyloferrin A in an Arginine-rich Binding PocketMycobacterium tuberculosis Rv0899 Adopts a Mixed α/β-Structure and Does Not Form a Transmembrane β-BarrelInsight into the Interaction of Metal Ions with TroA from Streptococcus suisA Molecular Mechanism for Bacterial Susceptibility to ZincEvidence for an ABC-Type Riboflavin Transporter System in Pathogenic SpirochetesArginine 116 stabilizes the entrance to the metal ion-binding site of the MntC proteinMetal Binding Is Critical for the Folding and Function of Laminin Binding Protein, Lmb of Streptococcus agalactiaeRole of the Two Structural Domains from the Periplasmic Escherichia coli Histidine-binding Protein HisJImperfect coordination chemistry facilitates metal ion release in the Psa permeaseAlignment of distantly related protein structures: algorithm, bound and implications to homology modelingMolecular basis of bacterial outer membrane permeability revisitedInsights into the potential function and membrane organization of the TP0435 (Tp17) lipoprotein from Treponema pallidum derived from structural and biophysical analysesSurface immunolabeling and consensus computational framework to identify candidate rare outer membrane proteins of Treponema pallidum.TP0453, a concealed outer membrane protein of Treponema pallidum, enhances membrane permeability.Zn(II) metabolism in prokaryotes.Molecular dynamics simulations reveal that apo-HisJ can sample a closed conformation.High Resolution Structures of Periplasmic Glucose-binding Protein of Pseudomonas putida CSV86 Reveal Structural Basis of Its Substrate SpecificityThe PnrA (Tp0319; TmpC) lipoprotein represents a new family of bacterial purine nucleoside receptor encoded within an ATP-binding cassette (ABC)-like operon in Treponema pallidum.MtsABC is important for manganese and iron transport, oxidative stress resistance, and virulence of Streptococcus pyogenesInteractions between TonB from Escherichia coli and the periplasmic protein FhuD.Crystal structure of Yersinia pestis virulence factor YfeA reveals two polyspecific metal-binding sitesThe Tp38 (TpMglB-2) lipoprotein binds glucose in a manner consistent with receptor function in Treponema pallidum.The tprK gene is heterogeneous among Treponema pallidum strains and has multiple allelesTwo plant bacteria, S. meliloti and Ca. Liberibacter asiaticus, share functional znuABC homologues that encode for a high affinity zinc uptake systemZnu is the predominant zinc importer in Yersinia pestis during in vitro growth but is not essential for virulenceBiological basis for syphilis.FhuD1, a ferric hydroxamate-binding lipoprotein in Staphylococcus aureus: a case of gene duplication and lateral transfer.
P2860
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P2860
Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone
description
1999 nî lūn-bûn
@nan
1999 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone
@ast
Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone
@en
Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone
@nl
type
label
Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone
@ast
Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone
@en
Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone
@nl
prefLabel
Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone
@ast
Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone
@en
Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone
@nl
P2093
P3181
P356
P1476
Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone
@en
P2093
P304
P3181
P356
10.1038/10677
P577
1999-07-01T00:00:00Z