1toa
From Proteopedia
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PERIPLASMIC ZINC BINDING PROTEIN TROA FROM TREPONEMA PALLIDUM
Overview
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.
About this Structure
1TOA is a Single protein structure of sequence from Treponema pallidum with ZN and GOL as ligands. Full crystallographic information is available from OCA.
Reference
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
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