Expression, crystallization and preliminary X-ray crystallographic analysis of alanine racemase from Acinetobacter baumannii OXA-23

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Sep;69(Pt 9):1041-4. doi: 10.1107/S1744309113022343. Epub 2013 Aug 21.

Abstract

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 P2(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%.

Keywords: Acinetobacter baumannii; PLP; alanine racemase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acinetobacter baumannii / chemistry*
  • Acinetobacter baumannii / enzymology
  • Acinetobacter baumannii / genetics
  • Alanine Racemase / chemistry*
  • Alanine Racemase / genetics
  • Alanine Racemase / isolation & purification
  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification
  • Crystallography, X-Ray
  • Escherichia coli / genetics
  • Gene Expression
  • Molecular Sequence Data
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification

Substances

  • Bacterial Proteins
  • Recombinant Proteins
  • Alanine Racemase