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Crystallization and preliminary X‐ray diffraction analysis of recombinant pentalenene synthase
Author(s) -
Lesburg Charles A.,
Lloyd Matthew D.,
Cane David E.,
Christianson David W.
Publication year - 1995
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560041124
Subject(s) - recombinant dna , crystallography , atp synthase , farnesyl pyrophosphate , stereochemistry , escherichia coli , chemistry , crystallization , resolution (logic) , enzyme , biochemistry , organic chemistry , gene , artificial intelligence , computer science
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 Å and c = 56.5 Å. Hexagonal prismatic crystals, approximately 0.2 × 0.2 × 0.3 mm, diffract to approximately 2.9 Å 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.