Structure of TTHA1623, a novel metallo-beta-lactamase superfamily protein from Thermus thermophilus HB8

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 May 1;65(Pt 5):455-9. doi: 10.1107/S174430910901361X. Epub 2009 Apr 24.

Abstract

TTHA1623 is a metallo-beta-lactamase superfamily protein from the extremely thermophilic bacterium Thermus thermophilus HB8. Homologues of TTHA1623 exist in a wide range of bacteria and archaea and one eukaryote, Giardia lamblia, but their function remains unknown. To analyze the structural properties of TTHA1623, the crystal structures of its iron-bound and zinc-bound forms have been determined to 2.8 and 2.2 A resolution, respectively. TTHA1623 possesses an alphabetabetaalpha-fold similar to that of other metallo-beta-lactamase superfamily proteins with glyoxalase II-type metal coordination. However, TTHA1623 exhibits a putative substrate-binding pocket with a unique shape.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallography, X-Ray
  • Metals / chemistry*
  • Metals / metabolism*
  • Models, Molecular
  • Protein Binding
  • Protein Structure, Tertiary
  • Structural Homology, Protein
  • Thermus thermophilus / enzymology*
  • Thermus thermophilus / genetics
  • beta-Lactamases / chemistry*
  • beta-Lactamases / classification
  • beta-Lactamases / genetics
  • beta-Lactamases / metabolism*

Substances

  • Metals
  • beta-Lactamases