Crystal structure of chorismate mutase from Burkholderia phymatum

Acta Crystallogr F Struct Biol Commun. 2018 Apr 1;74(Pt 4):187-192. doi: 10.1107/S2053230X18002868. Epub 2018 Mar 22.


The bacterium Burkholderia phymatum is a promiscuous symbiotic nitrogen-fixating bacterium that belongs to one of the largest groups of Betaproteobacteria. Other Burkholderia species are known to cause disease in plants and animals, and some are potential agents for biological warfare. Structural genomics efforts include characterizing the structures of enzymes from pathways that can be targeted for drug development. As part of these efforts, chorismate mutase from B. phymatum was produced and crystallized, and a 1.95 Å resolution structure is reported. This enzyme shares less than 33% sequence identity with other homologs of known structure. There are two classes of chorismate mutase: AroQ and AroH. The bacterial subclass AroQγ has reported roles in virulence. Chorismate mutase from B. phymatum has the prototypical AroQγ topology and retains the characteristic chorismate mutase active site. This suggests that substrate-based chorismate mutase inhibitors will not be specific and are likely to affect beneficial bacteria such as B. phymatum.

Keywords: Burkholderia phymatum; Seattle Structural Genomics Center for Infectious Disease; chorismate mutase; isomerase; shikimate pathway; structural genomics.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Sequence
  • Burkholderiaceae / enzymology*
  • Catalytic Domain
  • Chorismate Mutase / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Models, Molecular
  • Protein Conformation
  • Sequence Homology


  • Chorismate Mutase