Purification, crystallization and preliminary X-ray crystallographic analysis of the UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase (MurF) from Acinetobacter baumannii

Acta Crystallogr F Struct Biol Commun. 2014 Jul;70(Pt 7):976-8. doi: 10.1107/S2053230X14009984. Epub 2014 Jun 19.

Abstract

The emergence and global spread of multidrug-resistant Acinetobacter baumannii strains are major threats to public health. Inhibition of peptidoglycan biosynthesis is an effective strategy for the development of antibiotics. The ATP-dependent UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase (MurF) that is responsible for the last step of peptidoglycan biosynthesis is a validated target for the development of antibiotics. Crystals of A. baumannii MurF in complex with ATP were grown by the microbatch crystallization method at 295 K. The crystals belonged to space group P322₁, with unit-cell parameters a=b=85.42, c=129.86 Å. Assuming the presence of one molecule in the asymmetric unit, the solvent content was estimated to be about 54.32%.

Keywords: Acinetobacter baumannii; MurF.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acinetobacter baumannii / chemistry*
  • Acinetobacter baumannii / enzymology
  • Adenosine Triphosphate / chemistry*
  • Amino Acid Sequence
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Gene Expression
  • Molecular Sequence Data
  • Peptide Synthases / chemistry*
  • Peptide Synthases / genetics
  • Peptide Synthases / metabolism
  • Peptidoglycan / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism

Substances

  • Peptidoglycan
  • Recombinant Proteins
  • Adenosine Triphosphate
  • Peptide Synthases
  • UDP-N-acetylmuramoylalanyl-D-glutamyllysine-D-alanyl-D-alanine ligase