4E79

Structure of LpxD from Acinetobacter baumannii at 2.66A resolution (P4322 form)

4E79 の概要

• エントリーDOI: 10.2210/pdb4e79/pdb
• 関連するPDBエントリー: 4E6T 4E6U 4E75
• 分子名称: UDP-3-O-acylglucosamine N-acyltransferase (2 entities in total)
• 機能のキーワード: lipopolysaccaride synthesis, transferase
• 由来する生物種: Acinetobacter baumannii
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 115417.45

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: 2013-01-16, 最終更新日: 2023-09-13)

主引用文献

Badger, J.,Chie-Leon, B.,Logan, C.,Sridhar, V.,Sankaran, B.,Zwart, P.H.,Nienaber, V.
Structure determination of LpxD from the lipopolysaccharide-synthesis pathway of Acinetobacter baumannii.
Acta Crystallogr.,Sect.F, 69:6-9, 2013

PubMed Abstract: Acinetobacter baumannii is a Gram-negative bacterium that is resistant to many currently available antibiotics. The protein LpxD is a component of the biosynthetic pathway for lipopolysaccharides in the outer membrane of this bacterium and is a potential target for new antibacterial agents. This paper describes the structure determination of apo forms of LpxD in space groups P2(1) and P4(3)22. These crystals contained six and three copies of the protein molecule in the asymmetric unit and diffracted to 2.8 and 2.7 Å resolution, respectively. A comparison of the multiple protein copies in the asymmetric units of these crystals reveals a common protein conformation and a conformation in which the relative orientation between the two major domains in the protein is altered.

PubMed: 23295477
DOI: 10.1107/S1744309112048890

実験手法

X-RAY DIFFRACTION (2.66 Å)