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B6db references: 224817733

type Journal Article
authors Oliver MR, Crowther JM, Leeman MM, Kessans SA, North RA, Donovan KA, Griffin MD, Suzuki H, Hudson AO, Kasanmascheff M, Dobson RC
title The purification, crystallization and preliminary X-ray diffraction analysis of two isoforms of meso-diaminopimelate decarboxylase from Arabidopsis thaliana
journal Acta Crystallogr F Struct Biol Commun.
sel selected
ui 224817733
year (2014)
volume 70
number 5
pages 663-8
keywords S-lysine; antibiotic resistance; antibiotics; diaminopimelate; diaminopimelate decarboxylase; drug discovery; herbicides; lysine biosynthesis
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 from a plant. The Arabidopsis thaliana diaminopimelate decarboxylase cDNAs At3g14390 (encoding DapDc1) and At5g11880 (encoding DapDc2) were cloned from genomic DNA and the recombinant proteins were expressed and purified from Escherichia coli Rosetta (DE3) cells. The crystals of DapDc1 and DapDc2 diffracted to beyond 2.00 and 2.27 resolution, respectively. Understanding the structural biology of diaminopimelate decarboxylase from a eukaryotic species will provide insights for the development of future herbicide treatments, in particular.
last changed 2017/07/24 15:48

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