1toa

PERIPLASMIC ZINC BINDING PROTEIN TROA FROM TREPONEMA PALLIDUM

spinqualitylabelsall models 1toa, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1toa is a 2 chain structure with sequence from "microspironema_pallidum"_(schaudinn_and_hoffmann_1905)_stiles_and_pfender_1905 "microspironema pallidum" (schaudinn and hoffmann 1905) stiles and pfender 1905. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TROA_TREPA] Part of an ATP-driven transport system TroABCD for zinc. Substrate-binding protein involved in the transport of zinc across the cytoplasmic membrane. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The crystal structure of recombinant TroA, a zinc-binding protein component of an ATP-binding cassette transport system in Treponema pallidum, was determined at a resolution of 1.8 A. The organization of the protein is largely similar to other periplasmic ligand-binding proteins (PLBP), in that two independent globular domains interact with each other to create a zinc-binding cleft between them. The structure has one bound zinc pentavalently coordinated to residues from both domains. Unlike previous PLBP structures that have an interdomain hinge composed of beta-strands, the N- and C-domains of TroA are linked by a single long backbone helix. This unique backbone helical conformation was possibly adopted to limit the hinge motion associated with ligand exchange. Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone.,Lee YH, Deka RK, Norgard MV, Radolf JD, Hasemann CA Nat Struct Biol. 1999 Jul;6(7):628-33. PMID:10404217 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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