Open AccessCrystallization and preliminary X‐ray analysis of the O ‐methyltransferase NovP from the novobiocin‐biosynthetic cluster of Streptomyces spheroides
Author(s) -
Stevenson Clare E. M.,
Freel Meyers Caren L.,
Walsh Christopher T.,
Lawson David M.
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107008287
Subject(s) - novobiocin , crystallization , streptomyces , methyltransferase , chemistry , cluster (spacecraft) , crystallography , stereochemistry , biochemistry , biology , genetics , methylation , organic chemistry , dna , antibiotics , bacteria , computer science , programming language
Crystals of recombinant NovP (subunit MW = 29 967 Da; 262 amino acids), an S ‐adenosyl‐ l ‐methionine‐dependent O ‐methyltransferase from Streptomyces spheroides , were grown by vapour diffusion. The protein crystallized in space group P 2, with unit‐cell parameters a = 51.81, b = 46.04, c = 61.22 Å, β = 104.97°. Native data to a maximum resolution of 1.4 Å were collected from a single crystal at the synchrotron. NovP is involved in the biosynthesis of the aminocoumarin antibiotic novobiocin that targets the essential bacterial enzyme DNA gyrase.