5U5I

The dimeric crystal structure of the selenomethionine derivative of HTPA Reductase from Sellaginella moellendorffii

Summary for 5U5I

• Entry DOI: 10.2210/pdb5u5i/pdb
• Related: 5U5N
• Descriptor: HTPA Reductase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: dhdpr, dihydrodipicolinate reductase, htpa reductase, oxidoreductase
• Biological source: Selaginella moellendorffii (Spikemoss)
• Total number of polymer chains: 2
• Total formula weight: 62594.34

Authors

Keown, J.R.,Goldstone, D.C.,Pearce, F.G. (deposition date: 2016-12-06, release date: 2017-12-06, Last modification date: 2024-10-30)

Primary citation

Watkin, S.A.J.,Keown, J.R.,Richards, E.,Goldstone, D.C.,Devenish, S.R.A.,Grant Pearce, F.
Plant DHDPR forms a dimer with unique secondary structure features that preclude higher-order assembly.
Biochem. J., 475:137-150, 2018

PubMed 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 (grape) and are dimeric in solution. In the present study, we have also determined the crystal structures of DHDPR enzymes from the plants and , 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 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.

PubMed: 29187521
DOI: 10.1042/BCJ20170709

Experimental method

X-RAY DIFFRACTION (2.2 Å)