Open AccessStructure determination of LpxD from the lipopolysaccharide‐synthesis pathway of Acinetobacter baumannii
Author(s) -
Badger John,
ChieLeon Barbara,
Logan Cheyenne,
Sridhar Vandana,
Sankaran Banumathi,
Zwart Peter H.,
Nienaber Vicki
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112048890
Subject(s) - acinetobacter baumannii , bacterial outer membrane , bacteria , lipopolysaccharide , antibiotics , microbiology and biotechnology , acinetobacter , chemistry , escherichia coli , biology , stereochemistry , biochemistry , pseudomonas aeruginosa , gene , genetics , endocrinology
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 P 2 1 and P 4 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.