Open AccessCrystallization and preliminary X‐ray analysis of dihydrodipicolinate synthase from Clostridium botulinum in the presence of its substrate pyruvate
Author(s) -
Atkinson Sarah C.,
Dobson Renwick C. J.,
Newman Janet M.,
Gorman Michael A.,
Dogovski Con,
Parker Michael W.,
Perugini Matthew A.
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108039018
Subject(s) - crystallization , crystallography , clostridium botulinum , chemistry , substrate (aquarium) , crystal (programming language) , psychrophile , resolution (logic) , monomer , enzyme , stereochemistry , biochemistry , biology , organic chemistry , toxin , ecology , artificial intelligence , computer science , programming language , polymer
In this paper, the crystallization and preliminary X‐ray diffraction analysis to near‐atomic resolution of DHDPS from Clostridium botulinum crystallized in the presence of its substrate pyruvate are presented. The enzyme crystallized in a number of forms using a variety of PEG precipitants, with the best crystal diffracting to 1.2 Å resolution and belonging to space group C 2, in contrast to the unbound form, which had trigonal symmetry. The unit‐cell parameters were a = 143.4, b = 54.8, c = 94.3 Å, β = 126.3°. The crystal volume per protein weight ( V M ) was 2.3 Å 3 Da −1 (based on the presence of two monomers in the asymmetric unit), with an estimated solvent content of 46%. The high‐resolution structure of the pyruvate‐bound form of C. botulinum DHDPS will provide insight into the function and stability of this essential bacterial enzyme.