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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)