5mlm

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

spinqualitylabelsall models 5mlm, resolution 2.56Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5mlm is a 1 chain structure with sequence from Plantago major. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.563Å Ligands: NAP, STR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D6N9X1_PLAMJ Publication Abstract from PubMed 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 5beta-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. A multisubstrate reductase from Plantago major: structure-function in the short chain reductase superfamily.,Fellows R, Russo CM, Silva CS, Lee SG, Jez JM, Chisholm JD, Zubieta C, Nanao MH Sci Rep. 2018 Oct 4;8(1):14796. doi: 10.1038/s41598-018-32967-1. PMID:30287897 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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