Open AccessPurification, crystallization and preliminary X‐ray crystallographic analysis of diaminopimelate epimerase from Acinetobacter baumannii
Author(s) -
Park Jeong Soon,
Lee Woo Cheol,
Song Jung Hyun,
Kim Seung Il,
Lee Je Chul,
Cheong Chaejoon,
Kim HyeYeon
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112048506
Subject(s) - acinetobacter baumannii , crystallization , microbiology and biotechnology , acinetobacter , crystallography , bacteria , materials science , chemistry , biology , antibiotics , genetics , pseudomonas aeruginosa , organic chemistry
The meso isomer of diaminopimelate ( meso ‐DAP) is a biosynthetic precursor of L‐lysine in bacteria and plants, and is a key component of the peptidoglycan layer in the cell walls of Gram‐negative and some Gram‐positive bacteria. Diaminopimelate epimerase (DapF) is a pyridoxal‐5′‐phosphate‐independent racemase which catalyses the interconversion of (6 S ,2 S )‐2,6‐diaminopimelic acid (LL‐DAP) and meso ‐DAP. In this study, DapF from Acinetobacter baumannii was overexpressed in Escherichia coli strain SoluBL21, purified and crystallized using a vapour‐diffusion method. A native crystal diffracted to a resolution of 1.9 Å and belonged to space group P 3 1 or P 3 2 , with unit‐cell parameters a = b = 74.91, c = 113.35 Å, α = β = 90, γ = 120°. There were two molecules in the asymmetric unit.