Crystallization and preliminary X-ray analysis of the aromatic prenyltransferase CloQ from the clorobiocin biosynthetic cluster of Streptomyces roseochromogenes.
Crystals of recombinant CloQ (subunit MW = 35 626 Da; 324 amino acids), an aromatic prenyltransferase from Streptomyces roseochromogenes, were grown by vapour diffusion. The protein crystallizes in space group I4(1)22, with unit-cell parameters a = b = 135.19, c = 98.13 A. Native data from a single crystal were recorded to a resolution of 2.2 A in-house. Preliminary analysis of these data indicated that the asymmetric unit corresponds to a monomer, giving an estimated solvent content of 60.6%. CloQ is involved in the biosynthesis of the aminocoumarin antibiotic clorobiocin, which targets the essential bacterial enzyme DNA gyrase.
Keller
Sascha
S
Department of Biological Chemistry, John Innes Centre, Norwich NR4 7UH, England, UK.
Pojer
Florence
F
Heide
Lutz
L
Lawson
David M
DM
D000900:Anti-Bacterial Agents / Q000096:biosynthesis; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification; D018360:Crystallography, X-Ray; D004122:Dimethylallyltranstransferase / Q000737:chemistry* / Q000302:isolation & purification; D009675:Novobiocin / Q000031:analogs & derivatives* / Q000096:biosynthesis; D013302:Streptomyces / Q000201:enzymology*
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D009675:Novobiocin; C006260:clorobiocin; D004122:Dimethylallyltranstransferase