X-ray crystal structure of Staphylococcus aureus FemA
X-ray crystal structure of Staphylococcus aureus FemA
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DOI：
10.1016/s0969-2126(02)00807-9
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发表时间：
2002-08-01
期刊：
影响因子：
5.7
通讯作者：
Garlick, RL
中科院分区：
文献类型：
--
作者：
Benson, TE;Prince, DB;Garlick, RL
葡萄球菌中肽聚糖生物合成的后期阶段涉及五肽赖氨酸侧链的epsilon氨基上五甘氨酸桥的合成。遗传和生物化学证据表明，这些甘氨酸的顺序添加是由三种同源酶催化的，FemX（FmhB），FemA和FemB。来自该家族的第一个蛋白质结构，金黄色葡萄球菌FemA，已经通过X射线晶体学以2.1埃分辨率解析。FemA结构揭示了参与肽和tRNA结合的几种已知蛋白质折叠的独特组织。蛋白质的表面还揭示了适合于肽聚糖底物的L形通道。对该酶结构特征的分析为阐明S. aureus FemA.
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 Angstrom 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.