Dihydrodipicolinate reductase (DHDPR) catalyses the second reaction in the diaminopimelate pathway of lysine biosynthesis in bacteria and plants. In contrast with the tetrameric bacterial DHDPR enzymes, we show that DHDPR from Vitis vinifera (grape) and Selaginella moellendorffii are dimeric in solution. In the present study, we have also determined the crystal structures of DHDPR enzymes from the plants Arabidopsis thaliana and S. moellendorffii, which are the first dimeric DHDPR structures. The analysis of these models demonstrates that the dimer forms through the intra-strand interface, and that unique secondary features in the plant enzymes block tetramer assembly. In addition, we have also solved the structure of tetrameric DHDPR from the pathogenic bacteria Neisseria meningitidis. Measuring the activity of plant DHDPR enzymes showed that they are much more prone to substrate inhibition than the bacterial enzymes, which appears to be a consequence of increased flexibility of the substrate-binding loop and higher affinity for the nucleotide substrate. This higher propensity to substrate inhibition may have consequences for ongoing efforts to increase lysine biosynthesis in plants.
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January 2018
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A 3D representation of the filamentous cyanobacteria Anabaena. In this issue, Sein-Echaluce et al. report on the molecular basis for the integration of environmental signals by FurB from Anabaena sp. PCC 7120; for details see pages 151–168.
Research Article|
January 05 2018
Plant DHDPR forms a dimer with unique secondary structure features that preclude higher-order assembly
Serena A.J. Watkin;
Serena A.J. Watkin
*
1Biomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, Christchurch, New Zealand
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Jeremy R. Keown;
Jeremy R. Keown
*
1Biomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, Christchurch, New Zealand
2School of Biological Sciences, University of Auckland, Auckland, New Zealand
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Eric Richards;
Eric Richards
1Biomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, Christchurch, New Zealand
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David C. Goldstone;
David C. Goldstone
2School of Biological Sciences, University of Auckland, Auckland, New Zealand
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Sean R.A. Devenish;
Sean R.A. Devenish
3Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA, U.K.
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F. Grant Pearce
1Biomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, Christchurch, New Zealand
Correspondence: Grant Pearce (grant.pearce@canterbury.ac.nz)
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Biochem J (2018) 475 (1): 137–150.
Article history
Received:
September 14 2017
Revision Received:
November 14 2017
Accepted:
November 28 2017
Accepted Manuscript online:
November 29 2017
Citation
Serena A.J. Watkin, Jeremy R. Keown, Eric Richards, David C. Goldstone, Sean R.A. Devenish, F. Grant Pearce; Plant DHDPR forms a dimer with unique secondary structure features that preclude higher-order assembly. Biochem J 15 January 2018; 475 (1): 137–150. doi: https://doi.org/10.1042/BCJ20170709
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