1TOA

PERIPLASMIC ZINC BINDING PROTEIN TROA FROM TREPONEMA PALLIDUM

Summary for 1TOA

• Entry DOI: 10.2210/pdb1toa/pdb
• Descriptor: PROTEIN (PERIPLASMIC BINDING PROTEIN TROA), ZINC ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: periplasmic binding protein, zinc binding protein, abc transporter, binding protein
• Biological source: Treponema pallidum
• Cellular location: Periplasm: P96116
• Total number of polymer chains: 2
• Total formula weight: 69246.77

Authors

Lee, Y.H.,Deka, R.K.,Norgard, M.V.,Radolf, J.D.,Hasemann, C.A. (deposition date: 1999-03-03, release date: 1999-07-05, Last modification date: 2023-12-27)

Primary citation

Lee, Y.H.,Deka, R.K.,Norgard, M.V.,Radolf, J.D.,Hasemann, C.A.
Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone.
Nat.Struct.Biol., 6:628-633, 1999

PubMed 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 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.

PubMed: 10404217
DOI: 10.1038/10677

Experimental method

X-RAY DIFFRACTION (1.8 Å)