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

DOI: 10.1107/S1744309112029144 DOI Help
PMID: 22869135 PMID Help

Authors: Daniel Tromans (John Innes Centre) , Clare Stevenson (John Innes Centre) , Rebecca J. M. Goss (University of East Anglia, U.K.) , David Lawson (John Innes Centre)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology And Crystallization Communications , VOL 68 (8) , PAGES 971 - 974

State: Published (Approved)
Published: August 2012
Diamond Proposal Number(s): 1219

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 Å from a single crystal. The crystal belonged to space group C2, with unit-cell parameters a = 214.12, b = 70.88, c = 142.22 Å, [beta] = 92.96°. Preliminary analysis of these data suggests that the asymmetric unit consists of one Pac17 homotetramer, with an estimated solvent content of 49.0%.

Journal Keywords: Pac17; Streptomyces; Pacidamycin; Antibiotic Biosynthesis; Diaminobutyric Acid

Subject Areas: Biology and Bio-materials, Chemistry, Medicine


Instruments: I02-Macromolecular Crystallography

Added On: 11/09/2012 09:34

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