1toa

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.