Abstract
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 Å. 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 β-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.
Original language | English (US) |
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Pages (from-to) | 628-633 |
Number of pages | 6 |
Journal | Nature Structural Biology |
Volume | 6 |
Issue number | 7 |
DOIs | |
State | Published - 1999 |
ASJC Scopus subject areas
- Structural Biology
- Biochemistry
- Genetics