CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION ANALYSIS OF RECOMBINANT PENTALENENE SYNTHASE

Recombinant pentalenene synthase, a 42.5-kDa sesquiterpene cyclase ori ginally isolated from Streptomyces UC5319 and cloned in Escherichia co li, has been crystallized in space group P6(3) with unit cell dimensio ns a = b = 183.5 Angstrom and c = 56.5 Angstrom. Hexagonal prismatic c rystals, approximately 0.2 x 0.2 x 0.3 mm, diffract to approximately 2 .9 Angstrom resolution using monochromatic synchrotron radiation. From the universal (and achiral) building block, farnesyl pyrophosphate, p entalenene synthase catalyzes the formation of four stereocenters in t he construction of the three fused five-membered rings of pentalenene; this novel sesquiterpene is a precursor to the pentalenolactone famil y of antibiotics.