Insights into TIM-barrel prenyl transferase mechanisms: crystal structures of PcrB from Bacillus subtilis and Staphylococcus aureus

Chembiochem. 2013 Jan 21;14(2):195-9. doi: 10.1002/cbic.201200748. Epub 2013 Jan 15.

Abstract

Well structured: As a new triose phosphate isomerase (TIM) barrel-fold prenyl transferase, PcrB catalyzes the production of heptaprenylglyceryl phosphate from heptaprenyl diphosphate and glycerol-1-phosphate. Crystal structures of PcrB from Bacillus subtilis and Staphylococcus aureus in complex with ligands were solved, and together with site-directed mutagenesis and bioinformatics analyses, clearly reveal the catalytic mechanism of the enzyme.

Publication types

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

MeSH terms

  • Alkyl and Aryl Transferases / chemistry*
  • Alkyl and Aryl Transferases / genetics
  • Alkyl and Aryl Transferases / metabolism
  • Bacillus subtilis / chemistry
  • Bacillus subtilis / enzymology*
  • Bacillus subtilis / genetics
  • Models, Molecular
  • Mutagenesis, Site-Directed
  • Protein Conformation
  • Staphylococcus aureus / chemistry
  • Staphylococcus aureus / enzymology*
  • Staphylococcus aureus / genetics
  • Triose-Phosphate Isomerase / chemistry*
  • Triose-Phosphate Isomerase / genetics
  • Triose-Phosphate Isomerase / metabolism

Substances

  • Alkyl and Aryl Transferases
  • Triose-Phosphate Isomerase