Crystallization and preliminary X-ray analysis of Pac17 from the pacidamycin-biosynthetic cluster of Streptomyces coeruleorubidus

Daniel R. Tromans, Clare E. M. Stevenson, Rebecca J. M. Goss, David M. Lawson*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Pac17 is an uncharacterized protein from the pacidamycin gene cluster of the soil bacterium Streptomyces coeruleorubidus. It is implicated in the biosynthesis of the core diaminobutyric acid residue of the antibiotic, although its precise role is uncertain at present. Given that pacidamycins inhibit translocase I of Pseudomonas aeruginosa, a clinically unexploited antibiotic target, they offer new hope in the search for antibacterial agents directed against this important pathogen. Crystals of Pac17 were grown by vapour diffusion and X-ray data were collected at a synchrotron to a resolution of 1.9 angstrom from a single crystal. The crystal belonged to space group C2, with unit-cell parameters a = 214.12, b = 70.88, c = 142.22 angstrom, beta = 92.96 degrees. Preliminary analysis of these data suggests that the asymmetric unit consists of one Pac17 homotetramer, with an estimated solvent content of 49.0%.

Original languageEnglish
Pages (from-to)971-974
Number of pages4
JournalActa Crystallographica. Section F, Structural biology and crystallization communications
Volume68
DOIs
Publication statusPublished - Aug 2012

Keywords

  • diaminobutyric acid
  • PEPTIDOGLYCAN SYNTHESIS
  • QUALITY
  • MODEL
  • pacidamycin
  • GENE-CLUSTER
  • IDENTIFICATION
  • Pac17
  • ANTIBIOTICS
  • antibiotic biosynthesis
  • Streptomyces coeruleorubidus
  • ACTINOPLANES-FRIULIENSIS

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