Purification, crystallization and preliminary X‐ray crystallographic analysis of diaminopimelate epimerase from Acinetobacter baumannii. Issue 1 (8th January 2013)

• Record Type: Journal Article
• Authors: Park, Jeong Soon; Lee, Woo Cheol; Song, Jung Hyun; Kim, Seung Il; Lee, Je Chul; Cheong, Chaejoon; Kim, Hye‐Yeon
• Is Part Of: Acta crystallographica. Volume 69:Issue 1(2013:Jan.)
• Page Start: 42
• Page End: 44
• Publication Date: 2013-01-08
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309112048506
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The <italic>meso</italic> isomer of diaminopimelate (<italic>meso</italic>‐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<italic>S</italic>, 2<italic>S</italic>)‐2, 6‐diaminopimelic acid (LL‐DAP) and <italic>meso</italic>‐DAP. In this study, DapF from <italic>Acinetobacter baumannii</italic> was overexpressed in <italic>Escherichia coli</italic> 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 <italic>P</italic>3₁ or <italic>P</italic>3₂, with unit‐cell parameters <italic>a</italic> = <italic>b</italic> = 74.91, <italic>c</italic> = 113.35 Å, α = β = 90, γ = 120°. There were two molecules in the asymmetric unit.</p> </abstract>