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

Gómez García Inmaculada | Zendy; Freel Meyers Caren L. | Zendy; Walsh Christopher T. | Zendy; Lawson David M. | Zendy

Open Access

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

Author(s) -

Gómez García Inmaculada,

Freel Meyers Caren L.,

Walsh Christopher T.,

Lawson David M.

Publication year - 2008

Publication title -

acta crystallographica section f

Language(s) - English

Resource type - Journals

ISSN - 1744-3091

DOI - 10.1107/s1744309108030145

Subject(s) - novobiocin , orthorhombic crystal system , dna gyrase , crystallography , crystallization , crystal (programming language) , biosynthesis , escherichia coli , biology , stereochemistry , chemistry , crystal structure , enzyme , biochemistry , antibiotics , gene , organic chemistry , computer science , programming language

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 C 2 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.

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