Structure and mechanism of glutamate racemase from Aquifex pyrophilus

Kwang Yeon Hwang, C. S. Cho, Suk Kim Sang Suk Kim, H. C. Sung, Gyu Yu Yeon Gyu Yu, Y. Cho

Research output: Contribution to journalArticle

95 Citations (Scopus)

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 Å resolution, reveals that the enzyme forms a dimer and each monomer consists of two α/β 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.

Original languageEnglish
Pages (from-to)422-426
Number of pages5
JournalNature Structural Biology
Volume6
Issue number5
DOIs
Publication statusPublished - 1999 May 19
Externally publishedYes

    Fingerprint

ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology
  • Genetics

Cite this

Hwang, K. Y., Cho, C. S., Sang Suk Kim, S. K., Sung, H. C., Yeon Gyu Yu, G. Y., & Cho, Y. (1999). Structure and mechanism of glutamate racemase from Aquifex pyrophilus. Nature Structural Biology, 6(5), 422-426. https://doi.org/10.1038/8223