1ZUW

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

1ZUW の概要

• エントリーDOI: 10.2210/pdb1zuw/pdb
• 分子名称: glutamate racemase 1, D-GLUTAMIC ACID (3 entities in total)
• 機能のキーワード: glutamate racemase; (r)-glutamate; peptidoglycan biosynthesis, isomerase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 90529.37

構造登録者

Ruzheinikov, S.N.,Taal, M.A.,Sedelnikova, S.E.,Baker, P.J.,Rice, D.W. (登録日: 2005-06-01, 公開日: 2005-12-06, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.75 Å)