Open AccessCrystallization and preliminary X‐ray analysis of the bacillaene synthase trans ‐acting acyltransferase PksC
Author(s) -
Cuskin Fiona,
Solovyova Alexandra S.,
Lewis Richard J.,
Race Paul R.
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111003484
Subject(s) - acyltransferase , acyltransferases , bacillus subtilis , atp synthase , orthorhombic crystal system , stereochemistry , biosynthesis , transferase , chemistry , polyketide synthase , enzyme , biochemistry , crystallography , biology , polyketide , crystal structure , genetics , bacteria
The antibiotic bacillaene is biosynthesized in Bacillus subtilis by a hybrid type 1 modular polyketide synthase/nonribosomal peptide synthetase of the trans ‐acyltransferase ( trans ‐AT) class. Within this system, the essential acyl‐group loading activity is provided by the action of three free‐standing trans ‐acting acyltransferases. Here, the recombinant expression, purification and crystallization of the bacillaene synthase trans ‐acting acyltransferase PksC are reported. A diffraction data set has been collected from a single PksC crystal to 1.44 Å resolution and the crystal was found to belong to the orthorhombic space group P 2 1 2 1 2 1 .