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- Title
Structure and mechanism of glutamate racemase from Aquifex pyrophilus.
- Authors
Hwang, K Y; Cho, C S; Kim, S S; Sung, H C; Yu, Y G; Cho, Y
- Abstract
Glutamate racemase (MurI) is responsible for the synthesis of D-glutamate, an essential building block of the peptidoglycan layer in bacterial cell walls. The crystal structure of glutamate racemase from Aquifex pyrophilus, determined at 2.3 A resolution, reveals that the enzyme forms a dimer and each monomer consists of two alpha/beta fold domains, a unique structure that has not been observed in other racemases or members of an enolase superfamily. A substrate analog, D-glutamine, binds to the deep pocket formed by conserved residues from two monomers. The structural and mutational analyses allow us to propose a mechanism of metal cofactor-independent glutamate racemase in which two cysteine residues are involved in catalysis.
- Publication
Nature structural biology, 1999, Vol 6, Issue 5, p422
- ISSN
1072-8368
- Publication type
Journal Article
- DOI
10.1038/8223