5UA0

Dimeric crystal structure of HTPA reductase from arabidopsis thaliana

5UA0 の概要

• エントリーDOI: 10.2210/pdb5ua0/pdb
• 分子名称: 4-hydroxy-tetrahydrodipicolinate reductase 2, chloroplastic, SULFATE ION (3 entities in total)
• 機能のキーワード: htpa reductase dhdpr lysine biosynthesis, oxidoreductase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• 細胞内の位置: Plastid, chloroplast : Q8LB01
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 107789.62

構造登録者

Keown, J.K.,Pearce, F.G.,Goldstone, D.C. (登録日: 2016-12-18, 公開日: 2017-12-13, 最終更新日: 2023-10-04)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.3 Å)