Open AccessStructure determination of LpxA 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 - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911204571x
Subject(s) - acinetobacter baumannii , acinetobacter , lipopolysaccharide , antibiotics , microbiology and biotechnology , bacteria , enzyme , bacterial outer membrane , chemistry , escherichia coli , stereochemistry , monomer , computational biology , biology , biochemistry , gene , genetics , organic chemistry , pseudomonas aeruginosa , polymer , endocrinology
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 P 2 1 2 1 2 1 and P 6 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 P 6 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.