4E6U

Structure of LpxA from Acinetobacter baumannii at 1.4A resolution (P63 form)

4E6U の概要

• エントリーDOI: 10.2210/pdb4e6u/pdb
• 関連するPDBエントリー: 4E6T 4E75 4E79
• 分子名称: Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase, SULFATE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: lipopolysaccaride synthesis, transferase
• 由来する生物種: Acinetobacter baumannii
• 細胞内の位置: Cytoplasm (By similarity): F0QHB3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29223.07

構造登録者

Badger, J.,Chie-Leon, B.,Logan, C.,Sridhar, V.,Sankaran, B.,Zwart, P.H.,Nienaber, V. (登録日: 2012-03-16, 公開日: 2012-12-12, 最終更新日: 2024-02-28)

主引用文献

Badger, J.,Chie-Leon, B.,Logan, C.,Sridhar, V.,Sankaran, B.,Zwart, P.H.,Nienaber, V.
Structure determination of LpxA from the lipopolysaccharide-synthesis pathway of Acinetobacter baumannii.
Acta Crystallogr.,Sect.F, 68:1477-1481, 2012

PubMed Abstract: Acinetobacter baumannii is a Gram-negative pathogenic bacterium which is resistant to most currently available antibiotics and that poses a significant health threat to hospital patients. LpxA is a key enzyme in the biosynthetic pathway of the lipopolysaccharides that are components of the bacterial outer membrane. It is a potential target for antibacterial agents that might be used to fight A. baumannii infections. This paper describes the structure determination of the apo form of LpxA in space groups P2(1)2(1)2(1) and P6(3). These crystal forms contained three and one protein molecules in the asymmetric unit and diffracted to 1.8 and 1.4 Å resolution, respectively. A comparison of the conformations of the independent protein monomers within and between the two crystal asymmetric units revealed very little structural variation across this set of structures. In the P6(3) crystal form the enzymatic site is exposed and is available for the introduction of small molecules of the type used in fragment-based drug discovery and structure-based lead optimization.

PubMed: 23192027
DOI: 10.1107/S174430911204571X

実験手法

X-RAY DIFFRACTION (1.41 Å)