La Trobe
84948_Christensen,J_2016.pdf (4.5 MB)

Structure and function of cyanobacterial DHDPS and DHDPR

Download (4.5 MB)
journal contribution
posted on 2023-02-09, 00:37 authored by JB Christensen, Tatiana Soares-da-CostaTatiana Soares-da-Costa, Pierre Faou, FG Pearce, S Panjikar, Matthew PeruginiMatthew Perugini
Lysine biosynthesis in bacteria and plants commences with a condensation reaction catalysed by dihydrodipicolinate synthase (DHDPS) followed by a reduction reaction catalysed by dihydrodipicolinate reductase (DHDPR). Interestingly, both DHDPS and DHDPR exist as different oligomeric forms in bacteria and plants. DHDPS is primarily a homotetramer in all species, but the architecture of the tetramer differs across kingdoms. DHDPR also exists as a tetramer in bacteria, but has recently been reported to be dimeric in plants. This study aimed to characterise for the first time the structure and function of DHDPS and DHDPR from cyanobacteria, which is an evolutionary important phylum that evolved at the divergence point between bacteria and plants. We cloned, expressed and purified DHDPS and DHDPR from the cyanobacterium Anabaena variabilis. The recombinant enzymes were shown to be folded by circular dichroism spectroscopy, enzymatically active employing the quantitative DHDPS-DHDPR coupled assay, and form tetramers in solution using analytical ultracentrifugation. Crystal structures of DHDPS and DHDPR from A. variabilis were determined at 1.92 Å and 2.83 Å, respectively, and show that both enzymes adopt the canonical bacterial tetrameric architecture. These studies indicate that the quaternary structure of bacterial and plant DHDPS and DHDPR diverged after cyanobacteria evolved.


M.A.P. and S.P. acknowledge the Australian Research Council for funding support (DP150103313) and T.P.S.C. the National Health and Medical Research Council of Australia for fellowship support (APP1091976).


Publication Date



Scientific Reports



Article Number





Nature Publishing Group



Rights Statement

© The Author(s) 2016 This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit

Usage metrics

    Journal Articles


    No categories selected