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Purification, crystallization and preliminary X-ray crystallographic analysis of diaminopimelate epimerase from Acinetobacter baumannii.


ABSTRACT: 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 P3(1) or P3(2), with unit-cell parameters a = b = 74.91, c = 113.35?Å, ? = ? = 90, ? = 120°. There were two molecules in the asymmetric unit.

SUBMITTER: Park JS 

PROVIDER: S-EPMC3539701 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary X-ray crystallographic analysis of diaminopimelate epimerase from Acinetobacter baumannii.

Park Jeong Soon JS   Lee Woo Cheol WC   Song Jung Hyun JH   Kim Seung Il SI   Lee Je Chul JC   Cheong Chaejoon C   Kim Hye Yeon HY  

Acta crystallographica. Section F, Structural biology and crystallization communications 20121220 Pt 1


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 So  ...[more]

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