Purification, crystallization and preliminary X‐ray crystallographic analysis of diaminopimelate epimerase from
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 (6S,2S)‐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 P31 or P32, 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.
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Document Type: Research Article
Publication date: January 1, 2013