Structure and mechanism of glutamate racemase from Aquifex pyrophilus
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- Title
- Structure and mechanism of glutamate racemase from Aquifex pyrophilus
- Authors
- Hwang, KY; Cho, CS; Kim, SS; Sung, HC; Yu, YG; Cho, YJ
- Date Issued
- 1999-05
- Publisher
- Nature Publishing Group
- 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 Angstrom 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.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/16310
- DOI
- 10.1038/8223
- ISSN
- 1072-8368
- Article Type
- Article
- Citation
- NATURE STRUCTURAL BIOLOGY, vol. 6, no. 5, page. 422 - 426, 1999-05
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