5MLR

Plantago Major multifunctional oxidoreductase V150M mutant in complex with citral and NADP+

5MLR の概要

• エントリーDOI: 10.2210/pdb5mlr/pdb
• 分子名称: Progesterone 5-beta-reductase, CHLORIDE ION, SODIUM ION, ... (6 entities in total)
• 機能のキーワード: progesterone reductase, iridoid synthase, sdr, enzyme evolution, oxidoreductase
• 由来する生物種: Plantago major (common plantain)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47950.14

構造登録者

Fellows, R.,Russo, C.M.,Lee, S.G.,Jez, J.M.,Chisholm, J.D.,Zubieta, C.,Nanao, M. (登録日: 2016-12-07, 公開日: 2018-08-01, 最終更新日: 2024-01-17)

主引用文献

Fellows, R.,Russo, C.M.,Silva, C.S.,Lee, S.G.,Jez, J.M.,Chisholm, J.D.,Zubieta, C.,Nanao, M.H.
A multisubstrate reductase from Plantago major: structure-function in the short chain reductase superfamily.
Sci Rep, 8:14796-14796, 2018

PubMed Abstract: The short chain dehydrogenase/reductase superfamily (SDR) is a large family of NAD(P)H-dependent enzymes found in all kingdoms of life. SDRs are particularly well-represented in plants, playing diverse roles in both primary and secondary metabolism. In addition, some plant SDRs are also able to catalyse a reductive cyclisation reaction critical for the biosynthesis of the iridoid backbone that contains a fused 5 and 6-membered ring scaffold. Mining the EST database of Plantago major, a medicinal plant that makes iridoids, we identified a putative 5β-progesterone reductase gene, PmMOR (P. major multisubstrate oxido-reductase), that is 60% identical to the iridoid synthase gene from Catharanthus roseus. The PmMOR protein was recombinantly expressed and its enzymatic activity assayed against three putative substrates, 8-oxogeranial, citral and progesterone. The enzyme demonstrated promiscuous enzymatic activity and was able to not only reduce progesterone and citral, but also to catalyse the reductive cyclisation of 8-oxogeranial. The crystal structures of PmMOR wild type and PmMOR mutants in complex with NADP or NAD and either 8-oxogeranial, citral or progesterone help to reveal the substrate specificity determinants and catalytic machinery of the protein. Site-directed mutagenesis studies were performed and provide a foundation for understanding the promiscuous activity of the enzyme.

PubMed: 30287897
DOI: 10.1038/s41598-018-32967-1

実験手法

X-RAY DIFFRACTION (1.46 Å)