4QF5

Crystal structure I of MurF from Acinetobacter baumannii

4QF5 の概要

• エントリーDOI: 10.2210/pdb4qf5/pdb
• 関連するPDBエントリー: 4QDI
• 分子名称: UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: udp-n-acetylmuramoyl-tripeptide-d-alanyl-d-ananine ligase, murf, ligase
• 由来する生物種: Acinetobacter baumannii
• 細胞内の位置: Cytoplasm : B7GVN5
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 104616.58

構造登録者

An, Y.J.,Jeong, C.S.,Cha, S.S. (登録日: 2014-05-19, 公開日: 2015-04-01, 最終更新日: 2025-03-26)

主引用文献

Cha, S.S.,An, Y.J.,Jeong, C.S.,Yu, J.H.,Chung, K.M.
ATP-binding mode including a carbamoylated lysine and two Mg(2+) ions, and substrate-binding mode in Acinetobacter baumannii MurF
Biochem.Biophys.Res.Commun., 450:1045-1050, 2014

PubMed Abstract: MurF adds d-Ala-d-Ala dipeptide to UDP-N-acetylmuramyl-l-Ala-γ-d-Glu-m-DAP (or l-Lys) in an ATP-dependent manner, which is the last step in the biosynthesis of monomeric precursor of peptidoglycan. Here we report crystal structures of two MurF-ATP complexes: the MurF-ATP complex and the MurF-ATP-UDP complex. The ATP-binding mode revealed by the crystal structure of the MurF-ATP complex confirms the previous biochemical demonstration that a carbamoylated lysine and two Mg(2+) ions are required for enzyme activity of MurF. The UDP-MurF interactions observed in the crystal structure of the MurF-ATP-UDP complex depict the characteristic substrate-binding mode of MurF. The emergence and dissemination of multidrug-resistant Acinetobacter baumannii strains are great threats to public health. Therefore, the structural information on A. baumannii MurF as a validated target for drug discovery will provide a framework to develop antibacterial agents against multidrug-resistant A. baumannii infections as well as to understand the reaction mechanism of MurF.

PubMed: 24978312
DOI: 10.1016/j.bbrc.2014.06.108

実験手法

X-RAY DIFFRACTION (2.8 Å)