Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone

Y. H. Lee, R. K. Deka, M. V. Norgard, J. D. Radolf, C. A. Hasemann

Research output: Contribution to journalArticlepeer-review

141 Scopus citations


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 languageEnglish (US)
Pages (from-to)628-633
Number of pages6
JournalNature Structural Biology
Issue number7
StatePublished - 1999

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics


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