1LRZ

x-ray crystal structure of staphylococcus aureus femA

Summary for 1LRZ

• Entry DOI: 10.2210/pdb1lrz/pdb
• Descriptor: factor essential for expression of methicillin resistance (2 entities in total)
• Functional Keywords: peptidoglycan, staphylococcus aureus, multiple anomalous dispersion, antibiotic inhibitor
• Biological source: Staphylococcus aureus
• Cellular location: Cytoplasm: P0A0A5
• Total number of polymer chains: 1
• Total formula weight: 50026.44

Authors

Benson, T.,Prince, D.,Mutchler, V.,Curry, K.,Ho, A.,Sarver, R.,Hagadorn, J.,Choi, G.,Garlick, R. (deposition date: 2002-05-16, release date: 2002-09-04, Last modification date: 2024-02-14)

Primary citation

Benson, T.E.,Prince, D.B.,Mutchler, V.T.,Curry, K.A.,Ho, A.M.,Sarver, R.W.,Hagadorn, J.C.,Choi, G.H.,Garlick, R.L.
X-ray crystal structure of Staphylococcus aureus FemA.
Structure, 10:1107-1115, 2002

PubMed 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.

PubMed: 12176388
DOI: 10.1016/S0969-2126(02)00807-9

Experimental method

X-RAY DIFFRACTION (2.1 Å)