Crystal structure of chorismate mutase from Burkholderia thailandensis

Acta Crystallogr F Struct Biol Commun. 2018 May 1;74(Pt 5):294-299. doi: 10.1107/S2053230X1800506X. Epub 2018 Apr 16.

Abstract

Burkholderia thailandensis is often used as a model for more virulent members of this genus of proteobacteria that are highly antibiotic-resistant and are potential agents of biological warfare that are infective by inhalation. As part of ongoing efforts to identify potential targets for the development of rational therapeutics, the structures of enzymes that are absent in humans, including that of chorismate mutase from B. thailandensis, have been determined by the Seattle Structural Genomics Center for Infectious Disease. The high-resolution structure of chorismate mutase from B. thailandensis was determined in the monoclinic space group P21 with three homodimers per asymmetric unit. The overall structure of each protomer has the prototypical AroQγ topology and shares conserved binding-cavity residues with other chorismate mutases, including those with which it has no appreciable sequence identity.

Keywords: Burkholderia thailandensis; Seattle Structural Genomics Center for Infectious Disease; chorismate mutase; isomerases; structural genomics.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Burkholderia / enzymology*
  • Burkholderia / genetics*
  • Chorismate Mutase / chemistry*
  • Chorismate Mutase / genetics*
  • Crystallization / methods
  • Protein Structure, Secondary

Substances

  • Chorismate Mutase