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5UA0

Dimeric crystal structure of HTPA reductase from arabidopsis thaliana

Summary for 5UA0
Entry DOI10.2210/pdb5ua0/pdb
Descriptor4-hydroxy-tetrahydrodipicolinate reductase 2, chloroplastic, SULFATE ION (3 entities in total)
Functional Keywordshtpa reductase dhdpr lysine biosynthesis, oxidoreductase
Biological sourceArabidopsis thaliana (Mouse-ear cress)
Cellular locationPlastid, chloroplast : Q8LB01
Total number of polymer chains3
Total formula weight107789.62
Authors
Keown, J.K.,Pearce, F.G.,Goldstone, D.C. (deposition date: 2016-12-18, release date: 2017-12-13, Last modification date: 2023-10-04)
Primary citationWatkin, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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数据于2024-10-30公开中

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