2UAG
UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE
2UAG の概要
| エントリーDOI | 10.2210/pdb2uag/pdb |
| 分子名称 | PROTEIN (UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE), MAGNESIUM ION, URIDINE-5'-DIPHOSPHATE-N-ACETYLMURAMOYL-L-ALANINE, ... (5 entities in total) |
| 機能のキーワード | ligase, peptidoglycan synthesis, murd, adp-forming enzyme |
| 由来する生物種 | Escherichia coli |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 48158.56 |
| 構造登録者 | |
| 主引用文献 | Bertrand, J.A.,Auger, G.,Martin, L.,Fanchon, E.,Blanot, D.,Le Beller, D.,van Heijenoort, J.,Dideberg, O. Determination of the MurD mechanism through crystallographic analysis of enzyme complexes. J.Mol.Biol., 289:579-590, 1999 Cited by PubMed Abstract: UDP -N- acetylmuramoyl- L -alanine: D -glutamate (MurD) ligase catalyses the addition of d -glutamate to the nucleotide precursor UDP -N- acetylmuramoyl- L -alanine (UMA). The crystal structures of three complexes of Escherichia coli MurD with a variety of substrates and products have been determined to high resolution. These include (1) the quaternary complex of MurD, the substrate UMA, the product ADP, and Mg2+, (2) the quaternary complex of MurD, the substrate UMA, the product ADP, and Mn2+, and (3) the binary complex of MurD with the product UDP - N- acetylmuramoyl- L -alanine- D -glutamate (UMAG). The reaction mechanism supported by these structures proceeds by the phosphorylation of the C-terminal carboxylate group of UMA by the gamma-phosphate group of ATP to form an acyl-phosphate intermediate, followed by the nucleophilic attack by the amino group of D-glutamate to produce UMAG. A key feature in the reaction intermediate is the presence of two magnesium ions bridging negatively charged groups. PubMed: 10356330DOI: 10.1006/jmbi.1999.2800 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.7 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






