1ZUW

Crystal structure of B.subtilis glutamate racemase (RacE) with D-Glu

Summary for 1ZUW

• Entry DOI: 10.2210/pdb1zuw/pdb
• Descriptor: glutamate racemase 1, D-GLUTAMIC ACID (3 entities in total)
• Functional Keywords: glutamate racemase; (r)-glutamate; peptidoglycan biosynthesis, isomerase
• Biological source: Bacillus subtilis
• Total number of polymer chains: 3
• Total formula weight: 90529.37

Authors

Ruzheinikov, S.N.,Taal, M.A.,Sedelnikova, S.E.,Baker, P.J.,Rice, D.W. (deposition date: 2005-06-01, release date: 2005-12-06, Last modification date: 2024-02-14)

Primary citation

Ruzheinikov, S.N.,Taal, M.A.,Sedelnikova, S.E.,Baker, P.J.,Rice, D.W.
Substrate-Induced Conformational Changes in Bacillus subtilis Glutamate Racemase and Their Implications for Drug Discovery
Structure, 13:1707-1713, 2005

PubMed Abstract: D-glutamate is an essential building block of the peptidoglycan layer in bacterial cell walls and can be synthesized from L-glutamate by glutamate racemase (RacE). The structure of a complex of B. subtilis RacE with D-glutamate reveals that the glutamate is buried in a deep pocket, whose formation at the interface of the enzyme's two domains involves a large-scale conformational rearrangement. These domains are related by pseudo-2-fold symmetry, which superimposes the two catalytic cysteine residues, which are located at equivalent positions on either side of the alpha carbon of the substrate. The structural similarity of these two domains suggests that the racemase activity of RacE arose as a result of gene duplication. The structure of the complex is dramatically different from that proposed previously and provides new insights into the RacE mechanism and an explanation for the potency of a family of RacE inhibitors, which have been developed as novel antibiotics.

PubMed: 16271894
DOI: 10.1016/j.str.2005.07.024

Experimental method

X-RAY DIFFRACTION (1.75 Å)