1P3D

Crystal Structure of UDP-N-acetylmuramic acid:L-alanine ligase (MurC) in Complex with UMA and ANP.

1P3D の概要

• エントリーDOI: 10.2210/pdb1p3d/pdb
• 関連するPDBエントリー: 1P31
• 分子名称: UDP-N-acetylmuramate--alanine ligase, MANGANESE (II) ION, URIDINE-5'-DIPHOSPHATE-N-ACETYLMURAMOYL-L-ALANINE, ... (5 entities in total)
• 機能のキーワード: alpha/beta protein, ligase
• 由来する生物種: Haemophilus influenzae
• 細胞内の位置: Cytoplasm : P45066
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 108254.31

構造登録者

Mol, C.D.,Brooun, A.,Dougan, D.R.,Hilgers, M.T.,Tari, L.W.,Wijnands, R.A.,Knuth, M.W.,McRee, D.E.,Swanson, R.V. (登録日: 2003-04-17, 公開日: 2003-07-15, 最終更新日: 2024-10-30)

主引用文献

Mol, C.D.,Brooun, A.,Dougan, D.R.,Hilgers, M.T.,Tari, L.W.,Wijnands, R.A.,Knuth, M.W.,McRee, D.E.,Swanson, R.V.
Crystal Structures of Active Fully Assembled Substrate- and Product-Bound Complexes of UDP-N-Acetylmuramic Acid:L-Alanine Ligase (MurC) from Haemophilus influenzae.
J.Bacteriol., 185:4152-4162, 2003

PubMed Abstract: UDP-N-acetylmuramic acid:L-alanine ligase (MurC) catalyzes the addition of the first amino acid to the cytoplasmic precursor of the bacterial cell wall peptidoglycan. The crystal structures of Haemophilus influenzae MurC in complex with its substrate UDP-N-acetylmuramic acid (UNAM) and Mg(2+) and of a fully assembled MurC complex with its product UDP-N-acetylmuramoyl-L-alanine (UMA), the nonhydrolyzable ATP analogue AMPPNP, and Mn(2+) have been determined to 1.85- and 1.7-A resolution, respectively. These structures reveal a conserved, three-domain architecture with the binding sites for UNAM and ATP formed at the domain interfaces: the N-terminal domain binds the UDP portion of UNAM, and the central and C-terminal domains form the ATP-binding site, while the C-terminal domain also positions the alanine. An active enzyme structure is thus assembled at the common domain interfaces when all three substrates are bound. The MurC active site clearly shows that the gamma-phosphate of AMPPNP is positioned between two bound metal ions, one of which also binds the reactive UNAM carboxylate, and that the alanine is oriented by interactions with the positively charged side chains of two MurC arginine residues and the negatively charged alanine carboxyl group. These results indicate that significant diversity exists in binding of the UDP moiety of the substrate by MurC and the subsequent ligases in the bacterial cell wall biosynthesis pathway and that alterations in the domain packing and tertiary structure allow the Mur ligases to bind sequentially larger UNAM peptide substrates.

PubMed: 12837790
DOI: 10.1128/JB.185.14.4152-4162.2003

実験手法

X-RAY DIFFRACTION (1.7 Å)