Structural, Bioinformatic, and In Vivo Analyses of Two Treponema pallidum Lipoproteins Reveal a Unique TRAP Transporter

Structural, Bioinformatic, and In Vivo Analyses of Two Treponema pallidum Lipoproteins Reveal a Unique TRAP Transporter

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http://www.wikidata.org/entity/Q27677054
Hypothetical Protein BB0569 Is Essential for Chemotaxis of the Lyme Disease Spirochete Borrelia burgdorferi.Evidence for an ABC-Type Riboflavin Transporter System in Pathogenic SpirochetesThe TP0796 Lipoprotein of Treponema pallidum Is a Bimetal-dependent FAD Pyrophosphatase with a Potential Role in Flavin HomeostasisStructural and Thermodynamic Characterization of the Interaction between Two Periplasmic Treponema pallidum Lipoproteins that are Components of a TPR-Protein-Associated TRAP Transporter (TPAT)Sequence, biophysical, and structural analyses of the PstS lipoprotein (BB0215) fromBorrelia burgdorferireveal a likely binding component of an ABC-type phosphate transporterInsights into the potential function and membrane organization of the TP0435 (Tp17) lipoprotein from Treponema pallidum derived from structural and biophysical analysesTripartite ATP-independent Periplasmic (TRAP) Transporters Use an Arginine-mediated Selectivity Filter for High Affinity Substrate Binding.Evidence for Posttranslational Protein Flavinylation in the Syphilis Spirochete Treponema pallidum: Structural and Biochemical Insights from the Catalytic Core of a Periplasmic Flavin-Trafficking ProteinThe Tp0684 (MglB-2) Lipoprotein of Treponema pallidum: A Glucose-Binding Protein with Divergent Topology.Molecular insights into the enzymatic diversity of flavin-trafficking protein (Ftp; formerly ApbE) in flavoprotein biogenesis in the bacterial periplasm.Purification, crystallization and preliminary X-ray analysis of TP0435 (Tp17) from the syphilis spirochete Treponema pallidum.Functional clues from the crystal structure of an orphan periplasmic ligand-binding protein from Treponema pallidum.Treponema pallidum, the syphilis spirochete: making a living as a stealth pathogen.The Treponema pallidum Outer Membrane.Tripartite ATP-Independent Periplasmic (TRAP) Transporters and Tripartite Tricarboxylate Transporters (TTT): From Uptake to Pathogenicity.Functional insights from proteome-wide structural modeling of Treponema pallidum subspecies pallidum, the causative agent of syphilis.
P2860

Structural, Bioinformatic, and In Vivo Analyses of Two Treponema pallidum Lipoproteins Reveal a Unique TRAP Transporter

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http://www.wikidata.org/entity/Q27677054
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2012 nî lūn-bûn
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2012 թուականի Մարտին հրատարակուած գիտական յօդուած
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2012 թվականի մարտին հրատարակված գիտական հոդված
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2012年の論文
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2012年論文
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2012年論文
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2012年論文
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2012年論文
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2012年論文
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2012年论文
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name
Structural, Bioinformatic, and ...... veal a Unique TRAP Transporter
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Structural, Bioinformatic, and ...... veal a Unique TRAP Transporter
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Structural, Bioinformatic, and ...... veal a Unique TRAP Transporter
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type
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Structural, Bioinformatic, and ...... veal a Unique TRAP Transporter
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Structural, Bioinformatic, and ...... veal a Unique TRAP Transporter
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Structural, Bioinformatic, and ...... veal a Unique TRAP Transporter
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Structural, Bioinformatic, and ...... veal a Unique TRAP Transporter
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Structural, Bioinformatic, and ...... veal a Unique TRAP Transporter
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Structural, Bioinformatic, and ...... veal a Unique TRAP Transporter
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Structural, Bioinformatic, and ...... veal a Unique TRAP Transporter
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P2093
P2860
P304
P31
P3181
P356
P407
P433
P478
P50
P577
P5875
P698
P921
P932