| Literature DB >> 22949190 |
Sarah C Atkinson1, Con Dogovski, Renwick C J Dobson, Matthew A Perugini.
Abstract
Dihydrodipicolinate synthase (DHDPS) catalyzes the first committed step of the lysine-biosynthesis pathway in bacteria, plants and some fungi. This study describes the cloning, expression, purification and crystallization of DHDPS (NP_354047.1) from the plant pathogen Agrobacterium tumefaciens (AgT-DHDPS). Enzyme-kinetics studies demonstrate that AgT-DHDPS possesses DHDPS activity in vitro. Crystals of AgT-DHDPS were grown in the unliganded form and in forms with substrate bound and with substrate plus allosteric inhibitor (lysine) bound. X-ray diffraction data sets were subsequently collected to a maximum resolution of 1.40 Å. Determination of the structure with and without substrate and inhibitor will offer insight into the design of novel pesticide agents.Entities:
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Year: 2012 PMID: 22949190 PMCID: PMC3433193 DOI: 10.1107/S1744309112033052
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091