8G6P

Crystal structure of Mycobacterium thermoresistibile MurE in complex with ADP and 2,6-Diaminopimelic acid

8G6P の概要

• エントリーDOI: 10.2210/pdb8g6p/pdb
• 分子名称: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase, MAGNESIUM ION, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: adp-binding ligase, cell wall biosynthesis, mure, m-dap complex, ligase
• 由来する生物種: Mycolicibacterium thermoresistibile
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 54106.44

構造登録者

Rossini, N.O.,Silva, C.S.,Dias, M.V.B. (登録日: 2023-02-15, 公開日: 2023-04-05, 最終更新日: 2023-11-15)

主引用文献

Rossini, N.O.,Silva, C.,Dias, M.V.B.
The crystal structure of Mycobacterium thermoresistibile MurE ligase reveals the binding mode of the substrate m-diaminopimelate.
J.Struct.Biol., 215:107957-107957, 2023

PubMed Abstract: The cytoplasmatic biosynthesis of the stem peptide from the peptidoglycan in bacteria involves six steps, which have the role of three ATP-dependent Mur ligases that incorporate three consecutive amino acids to a substrate precursor. MurE is the last Mur ligase to incorporate a free amino acid. Although the structure of MurE from Mycobacterium tuberculosis (MtbMurE) was determined at 3.0 Å, the binding mode of meso-Diaminopimelate (m-DAP) and the effect of substrate absence is unknown. Herein, we show the structure of MurE from M. thermoresistibile (MthMurE) in complex with ADP and m-DAP at 1.4 Å resolution. The analysis of the structure indicates key conformational changes that the substrate UDP-MurNAc-L-Ala-D-Glu (UAG) and the free amino acid m-DAP cause on the MthMurE conformation. We observed several movements of domains or loop regions that displace their position in order to perform enzymatic catalysis. Since MthMurE has a high similarity to MtbMurE, this enzyme could also guide strategies for structure-based antimicrobial discovery to fight against tuberculosis or other mycobacterial infections.

PubMed: 36944394
DOI: 10.1016/j.jsb.2023.107957

実験手法

X-RAY DIFFRACTION (1.45 Å)