2J65

Structure of LpxC from Aquifex aeolicus in complex with UDP

2J65 の概要

• エントリーDOI: 10.2210/pdb2j65/pdb
• 関連するPDBエントリー: 1P42 1XXE 1YH8 1YHC 2GO3 2GO4
• 分子名称: UDP-3-O-[3-HYDROXYMYRISTOYL] N-ACETYLGLUCOSAMINE DEACETYLASE, ZINC ION, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: hydrolase, lipid synthesis, lipid a biosynthesis
• 由来する生物種: AQUIFEX AEOLICUS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64001.22

構造登録者

Buetow, L.,Dawson, A.,Hunter, W.N. (登録日: 2006-09-26, 公開日: 2006-11-08, 最終更新日: 2023-12-13)

主引用文献

Buetow, L.,Dawson, A.,Hunter, W.N.
The Nucleotide-Binding Site of Aquifex Aeolicus Lpxc.
Acta Crystallogr.,Sect.F, 62:1082-, 2006

PubMed Abstract: The structure of recombinant Aquifex aeolicus UDP-3-O-acyl-N-acetylglucosamine deacetylase (LpxC) in complex with UDP has been determined to a resolution of 2.2 A. Previous studies have characterized the binding sites of the fatty-acid and sugar moieties of the substrate, UDP-(3-O-hydroxymyristoyl)-N-acetylglucosamine, but not that of the nucleotide. The uracil-binding site is constructed from amino acids that are highly conserved across species. Hydrophobic associations with the Phe155 and Arg250 side chains in combination with hydrogen-bonding interactions with the main chain of Glu154 and the side chains of Tyr151 and Lys227 position the base. The phosphate and ribose groups are directed away from the active site and interact with Arg137, Lys156, Glu186 and Arg250. The orientation of the phosphate-ribose tail is not conducive to catalysis, perhaps owing to the position of an inhibitory Zn(2+). However, based on the position of uracil revealed in this study and on the previously reported complex of LpxC with an inhibitor, a model is proposed for substrate binding.

PubMed: 17077484
DOI: 10.1107/S1744309106041893

実験手法

X-RAY DIFFRACTION (2.2 Å)