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Protein Sci. 1995 Nov;4(11):2436-8.

Crystallization and preliminary X-ray diffraction analysis of recombinant pentalenene synthase.

Author information

1
Department of Chemistry, University of Pennsylvania, Philadelphia 19104, USA.

Abstract

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.

PMID:
8563643
PMCID:
PMC2143018
DOI:
10.1002/pro.5560041124
[Indexed for MEDLINE]
Free PMC Article

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