Journal article
The purification, crystallization and preliminary X-ray diffraction analysis of two isoforms of meso-diaminopimelate decarboxylase from Arabidopsis thaliana
MR Oliver, JM Crowther, MM Leeman, SA Kessans, RA North, KA Donovan, MDW Griffin, H Suzuki, AO Hudson, M Kasanmascheff, RCJ Dobson
Acta Crystallographica Section F Structural Biology Communications | INT UNION CRYSTALLOGRAPHY | Published : 2014
Abstract
Diaminopimelate decarboxylase catalyses the last step in the diaminopimelate-biosynthetic pathway leading to S-lysine: the decarboxylation of meso-diaminopimelate to form S-lysine. Lysine biosynthesis occurs only in microorganisms and plants, and lysine is essential for the growth and development of animals. Thus, the diaminopimelate pathway represents an attractive target for antimicrobial and herbicide treatments and has received considerable attention from both a mechanistic and a structural viewpoint. Diaminopimelate decarboxylase has only been characterized in prokaryotic species. This communication describes the first structural studies of two diaminopimelate decarboxylase isoforms fro..
View full abstractGrants
Awarded by New Zealand Royal Society Marsden Fund
Awarded by US Army Research Office
Awarded by National Science Foundation (NSF) award (MCB)
Awarded by Div Of Molecular and Cellular Bioscience; Direct For Biological Sciences
Funding Acknowledgements
We acknowledge the support and assistance of the friendly staff at the CSIRO Collaborative Crystallization Centre at CSIRO Material Science and Engineering, Parkville, Melbourne and the MX beamline scientists at the Australian Synchrotron, Victoria, Australia. Parts of this research were undertaken at the MX2 beamline of the Australian Synchrotron, Victoria, Australia. Travel to the Australian Synchrotron was supported by the New Zealand Synchrotron Group. HS acknowledges the 2012 Researcher Exchange Program between JSPS and RSNZ. RCJD acknowledges (i) the New Zealand Royal Society Marsden Fund for funding support, in part (contract UOC1013), and (ii) the US Army Research Laboratory and US Army Research Office under contract/grant No. W911NF-11-1-0481 for support, in part. AOH acknowledges a National Science Foundation (NSF) award (MCB-#1120541) and a Rochester Institute of Technology (RIT) College of Science 2012 Dean's Research Initiation Grant. MML was supported by the NSF award to AOH. MDWG is the recipient of the C. R. Roper Fellowship. We especially thank Jackie Healy for her technical support.