1UAG

UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE

1UAG の概要

• エントリーDOI: 10.2210/pdb1uag/pdb
• 分子名称: UDP-N-ACETYLMURAMOYL-L-ALANINE/:D-GLUTAMATE LIGASE, SULFATE ION, URIDINE-5'-DIPHOSPHATE-N-ACETYLMURAMOYL-L-ALANINE, ... (4 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
• 細胞内の位置: Cytoplasm: P14900
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47874.87

構造登録者

Bertrand, J.,Fanchon, E.,Dideberg, O. (登録日: 1997-03-13, 公開日: 1998-03-18, 最終更新日: 2025-03-26)

主引用文献

Bertrand, J.A.,Auger, G.,Fanchon, E.,Martin, L.,Blanot, D.,van Heijenoort, J.,Dideberg, O.
Crystal structure of UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli.
EMBO J., 16:3416-3425, 1997

PubMed Abstract: UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase (MurD) is a cytoplasmic enzyme involved in the biosynthesis of peptidoglycan which catalyzes the addition of D-glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). The crystal structure of MurD in the presence of its substrate UMA has been solved to 1.9 A resolution. Phase information was obtained from multiple anomalous dispersion using the K-shell edge of selenium in combination with multiple isomorphous replacement. The structure comprises three domains of topology each reminiscent of nucleotide-binding folds: the N- and C-terminal domains are consistent with the dinucleotide-binding fold called the Rossmann fold, and the central domain with the mononucleotide-binding fold also observed in the GTPase family. The structure reveals the binding site of the substrate UMA, and comparison with known NTP complexes allows the identification of residues interacting with ATP. The study describes the first structure of the UDP-N-acetylmuramoyl-peptide ligase family.

PubMed: 9218784
DOI: 10.1093/emboj/16.12.3416

実験手法

X-RAY DIFFRACTION (1.95 Å)