Crystallization and preliminary X-ray analysis of the O-methyltransferase NovP from the novobiocin-biosynthetic cluster of Streptomyces spheroides.
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 P2, with unit-cell parameters a = 51.81, b = 46.04, c = 61.22 A, beta = 104.97 degrees. Native data to a maximum resolution of 1.4 A 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.
Stevenson
Clare E M
CE
Department of Biological Chemistry, John Innes Centre, Norwich NR4 7UH, England.
Freel Meyers
Caren L
CL
Walsh
Christopher T
CT
Lawson
David M
DM
D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D005810:Multigene Family; D009675:Novobiocin / Q000096:biosynthesis* / Q000737:chemistry* / Q000302:isolation & purification; D011497:Protein O-Methyltransferase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D013302:Streptomyces / Q000201:enzymology* / Q000235:genetics
D009675:Novobiocin; D011497:Protein O-Methyltransferase