Open AccessExpression, crystallization and preliminary X‐ray crystallographic analysis of alanine racemase from Acinetobacter baumannii OXA‐23
Author(s) -
Nguyen DinhDuc,
Ngo HoPhuongThuy,
Hong Myoungki,
Pham TanViet,
Lee Jung Hun,
Lee Jae Jin,
Kwon Dae Beom,
Lee Sang Hee,
Kang LinWoo
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113022343
Subject(s) - acinetobacter baumannii , orthorhombic crystal system , racemization , alanine , stereochemistry , crystallization , chemistry , cofactor , biochemistry , crystallography , crystal structure , biology , bacteria , amino acid , enzyme , organic chemistry , genetics , pseudomonas aeruginosa
Acinetobacter baumannii has received much attention owing to its exceptional ability to develop resistance to currently available antibiotics. Alanine racemase (ALR) catalyzes the racemization of L‐alanine to D‐alanine with pyridoxal 5′‐phosphate (PLP) as a cofactor. The D‐alanine product is an essential component of the bacterial cell wall and ALR is a potential target for the development of novel antibacterial drugs. The alr gene from A. baumannii was cloned and the protein (AbALR) was expressed, purified and crystallized. The AbALR crystal diffracted to 2.3 Å resolution and belonged to the primitive orthorhombic space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 55.1, b = 85.0, c = 167.7 Å. Two protomers were present in the asymmetric unit, with a corresponding V M value of 2.3 Å 3 Da −1 and a solvent content of 47.5%.