Crystallization and preliminary X-ray analysis of the O-carbamoyltransferase NovN from the novobiocin-biosynthetic cluster of Streptomyces spheroides

DOI: 10.1107/S1744309108030145
PMID: 18997325

Authors: Inmaculada Gómez García (John Innes Centre) , Caren L. Freel Meyers (Harvard Medical School) , Christopher T. Walsh (Harvard Medical School) , David M. Lawson (John Innes Centre)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology And Crystallization Communications , VOL 64 , PAGES 1000-1002

State: Published (Approved)
Published: September 2008
Diamond Proposal Number(s): 1219

Abstract: Crystals of recombinant NovN, an O-carbamoyltransferase from Streptomyces spheroides, were grown by vapour diffusion. The protein crystallized in two different crystal forms. Crystal form I belonged to space group C2 and native data were collected to 2.9 Å resolution in-house. Crystal form II had I-centred orthorhombic symmetry and native data were recorded to a resolution of 2.3 Å at a synchrotron. NovN catalyses the final step in the biosynthesis of the aminocoumarin antibiotic novobiocin that targets the essential bacterial enzyme DNA gyrase.

Journal Keywords: NovN; O-carbamoyltransferases; Streptomyces; novobiocin; antibiotic biosynthesis

Diamond Keywords: Bacteria; Enzymes

Subject Areas: Biology and Bio-materials, Medicine


Instruments: I02-Macromolecular Crystallography

Added On: 29/09/2010 20:14

Discipline Tags:

Health & Wellbeing Structural biology Drug Discovery Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)