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Plant DHDPR forms a dimer with unique secondary structure features that preclude higher-order assembly
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Watkin, Serena A. J., Keown, Jeremy R., Richards, Eric, Goldstone, David C., Devenish, Sean R. A. and Grant Pearce, F. (2018) Plant DHDPR forms a dimer with unique secondary structure features that preclude higher-order assembly. Biochemical Journal, 475 (1). pp. 137-150. doi:10.1042/BCJ20170709 ISSN 0264-6021.
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Official URL: http://doi.org/10.1042/BCJ20170709
Abstract
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.
Item Type: | Journal Article | ||||
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||
Journal or Publication Title: | Biochemical Journal | ||||
Publisher: | Portland Press | ||||
ISSN: | 0264-6021 | ||||
Official Date: | January 2018 | ||||
Dates: |
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Volume: | 475 | ||||
Number: | 1 | ||||
Page Range: | pp. 137-150 | ||||
DOI: | 10.1042/BCJ20170709 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access |
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