Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition state analog

Yuh Min Chook, Hengming Ke, William N. Lipscomb

Research output: Contribution to journalArticle

167 Scopus citations


We have solved the structure of a chorismate mutase (chorismate pyruvatemutase, EC, the 1.9-Å crystal structure of the monofunctional enzyme from Bacillus subtilis. The structure determination process was an unusual one, involving 12 monomers of the enzyme in the asymmetric unit. This structure was solved by the multiple isomorphous replacement method with partial structure phase combination and molecular averaging. The final model, which includes 1380 residues and 522 water molecules in an asymmetric unit, has been refined at 1.9 Å and the current crystallographic R value is 0.201. The B. subtilis chorismate mutase is a homotrimer, with β-sheets from each monomer packing to form the core of a pseudo-αβ-barrel with helices on the outside of the trimer. In addition, the active sites have been located by using data from a complex with an endo-oxabicyclic inhibitor that mimics the transition state of the reaction. The structure of this complex has been refined to 2.2 Å with a current R value of 0.182 for a model that includes 1388 residues, 12 inhibitor molecules, and 530 water molecules in the asymmetric unit. In each trimer, three equivalent active sites are located at the interfaces of two adjacent summits.

Original languageEnglish (US)
Pages (from-to)8600-8603
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number18
Publication statusPublished - Sep 15 1993



  • Claisen rearrangement
  • Shikimate pathway
  • X-ray crystallography

ASJC Scopus subject areas

  • General
  • Genetics

Cite this