1B74
GLUTAMATE RACEMASE FROM AQUIFEX PYROPHILUS
1B74 の概要
| エントリーDOI | 10.2210/pdb1b74/pdb |
| 関連するPDBエントリー | 1B73 |
| 分子名称 | GLUTAMATE RACEMASE, D-GLUTAMINE (3 entities in total) |
| 機能のキーワード | racemase, isomerase |
| 由来する生物種 | Aquifex pyrophilus |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 28124.85 |
| 構造登録者 | Hwang, K.Y.,Cho, C.S.,Kim, S.S.,Yu, Y.G.,Cho, Y. (登録日: 1999-01-27, 公開日: 2000-01-28, 最終更新日: 2023-12-27) |
| 主引用文献 | 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 Cited by 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: 10331867DOI: 10.1038/8223 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.3 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






