1toa
From Proteopedia
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. 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 Page seeded by OCA on Sat May 3 10:10:54 2008
