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

Young Jun An, Chang Sook Jeong, Jeong Hee Yu, Kyung Min Chung, Sun Shin Cha

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

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%.

Original languageEnglish
Pages (from-to)976-978
Number of pages3
JournalActa Crystallographica Section F:Structural Biology Communications
Volume70
Issue number7
DOIs
StatePublished - Jul 2014

Keywords

  • Acinetobacter baumannii
  • MurF

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