X-ray crystal structure of Staphylococcus aureus FemA

被引：68

作者：

Benson, TE

Prince, DB

Mutchler, VT

Curry, KA

Ho, AM

Sarver, RW

Hagadorn, JC

Choi, GH

Garlick, RL

机构：

[1] Pharmacia Corp, Struct Analyt & Med Chem, Kalamazoo, MI 49007 USA

[2] Pharmacia Corp, Prot Sci, Kalamazoo, MI 49007 USA

[3] Pharmacia Corp, Infect Dis Biol, Kalamazoo, MI 49007 USA

[4] Human Genome Sci, Rockville, MD 20850 USA

来源：

STRUCTURE | 2002年 / 10卷 / 08期

关键词：

FemA; peptidoglycan; Staphylococcus aureus; tRNA; binding; X-ray crystallography; multiple anomalous dispersion;

D O I：

10.1016/S0969-2126(02)00807-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：1107 / 1115

页数：9

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