Crystallization and preliminary X-ray diffraction analysis of recombinant pentalenene synthase.
Recombinant pentalenene synthase, a 42.5-kDa sesquiterpene cyclase originally isolated from Streptomyces UC5319 and cloned in Escherichia coli, has been crystallized in space group P6(3) with unit cell dimensions a = b = 183.5 A and c = 56.5 A. Hexagonal prismatic crystals, approximately 0.2 x 0.2 x 0.3 mm, diffract to approximately 2.9 A resolution using monochromatic synchrotron radiation. From the universal (and achiral) building block, farnesyl pyrophosphate, pentalenene synthase catalyzes the formation of four stereocenters in the construction of the three fused five-membered rings of pentalenene; this novel sesquiterpene is a precursor to the pentalenolactone family of antibiotics.
Lesburg
C A
CA
Department of Chemistry, University of Pennsylvania, Philadelphia 19104, USA.
Lloyd
M D
MD
Cane
D E
DE
Christianson
D W
DW
D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology; D019753:Intramolecular Lyases; D007535:Isomerases / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D013302:Streptomyces / Q000201:enzymology
D011994:Recombinant Proteins; D007535:Isomerases; D019753:Intramolecular Lyases; C048278:farnesylpyrophosphate cyclase