1LRZ

x-ray crystal structure of staphylococcus aureus femA

1LRZ の概要

• エントリーDOI: 10.2210/pdb1lrz/pdb
• 分子名称: factor essential for expression of methicillin resistance (2 entities in total)
• 機能のキーワード: peptidoglycan, staphylococcus aureus, multiple anomalous dispersion, antibiotic inhibitor
• 由来する生物種: Staphylococcus aureus
• 細胞内の位置: Cytoplasm: P0A0A5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 50026.44

構造登録者

Benson, T.,Prince, D.,Mutchler, V.,Curry, K.,Ho, A.,Sarver, R.,Hagadorn, J.,Choi, G.,Garlick, R. (登録日: 2002-05-16, 公開日: 2002-09-04, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.1 Å)