1B74

GLUTAMATE RACEMASE FROM AQUIFEX PYROPHILUS

Summary for 1B74

• Entry DOI: 10.2210/pdb1b74/pdb
• Related: 1B73
• Descriptor: GLUTAMATE RACEMASE, D-GLUTAMINE (3 entities in total)
• Functional Keywords: racemase, isomerase
• Biological source: Aquifex pyrophilus
• Total number of polymer chains: 1
• Total formula weight: 28124.85

Authors

Hwang, K.Y.,Cho, C.S.,Kim, S.S.,Yu, Y.G.,Cho, Y. (deposition date: 1999-01-27, release date: 2000-01-28, Last modification date: 2023-12-27)

Primary citation

Hwang, K.Y.,Cho, C.S.,Kim, S.S.,Sung, H.C.,Yu, Y.G.,Cho, Y.
Structure and mechanism of glutamate racemase from Aquifex pyrophilus.
Nat.Struct.Biol., 6:422-426, 1999

PubMed 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.

PubMed: 10331867
DOI: 10.1038/8223

Experimental method

X-RAY DIFFRACTION (2.3 Å)