X-ray crystal structure of Staphylococcus aureus FemA

Structure. 2002 Aug;10(8):1107-15. doi: 10.1016/s0969-2126(02)00807-9.

Abstract

The latter stages of peptidoglycan biosynthesis in Staphylococci involve the synthesis of a pentaglycine bridge on the epsilon amino group of the pentapeptide lysine side chain. Genetic and biochemical evidence suggest that sequential addition of these glycines is catalyzed by three homologous enzymes, FemX (FmhB), FemA, and FemB. The first protein structure from this family, Staphylococcus aureus FemA, has been solved at 2.1 A resolution by X-ray crystallography. The FemA structure reveals a unique organization of several known protein folds involved in peptide and tRNA binding. The surface of the protein also reveals an L-shaped channel suitable for a peptidoglycan substrate. Analysis of the structural features of this enzyme provides clues to the mechanism of action of S. aureus FemA.

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Crystallography, X-Ray
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Structure
  • Peptidoglycan / biosynthesis
  • Protein Structure, Tertiary*
  • Sequence Alignment
  • Staphylococcus aureus / enzymology*

Substances

  • Bacterial Proteins
  • FemA protein, Bacteria
  • Peptidoglycan

Associated data

  • PDB/1LRZ