8a3n

Geissoschizine synthase from Catharanthus roseus - binary complex with NADP+

spinqualitylabelsall models 8a3n, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8a3n is a 2 chain structure with sequence from Catharanthus roseus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: NAP, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GS_CATRO Component of the seco-iridoid and derivatives monoterpenoid indole alkaloids (MIAs, e.g. catharanthine, tabersonine, vincadifformine, vindoline, vincristine, quinine and strychnine) biosynthesis pathway. Catalyzes iminium reduction on 4,21-dehydrogeissoschizine to produce 19E-geissoschizine, precursor of catharanthine and tabersonine derivatives (PubMed:29147812, PubMed:30256480). May also catalyze the production of reactive intermediate used by the HL1, HL2, HL3 and HL4 to form catharanthine, vincadifformine and tabersonine (PubMed:30256480). Publication Abstract from PubMed Medium-chain alcohol dehydrogenases (ADHs) comprise a highly conserved enzyme family that catalyse the reversible reduction of aldehydes. However, recent discoveries in plant natural product biosynthesis suggest that the catalytic repertoire of ADHs has been expanded. Here we report the crystal structure of dihydroprecondylocarpine acetate synthase (DPAS), an ADH that catalyses the non-canonical 1,4-reduction of an alpha,beta -unsaturated iminium moiety. Comparison with structures of plant-derived ADHs suggest the 1,4-iminium reduction does not require a proton relay or the presence of a catalytic zinc ion in contrast to canonical 1,2-aldehyde reducing ADHs that require the catalytic zinc and a proton relay. Furthermore, ADHs that catalysed 1,2-iminium reduction required the presence of the catalytic zinc and the loss of the proton relay. This suggests how the ADH active site can be modified to perform atypical carbonyl reductions, providing insight into how chemical reactions are diversified in plant metabolism. Expansion of the Catalytic Repertoire of Alcohol Dehydrogenases in Plant Metabolism.,Langley C, Tatsis E, Hong B, Nakamura Y, Paetz C, Stevenson CE, Basquin J, Lawson DM, Caputi L, O'Connor SE Angew Chem Int Ed Engl. 2022 Oct 5. doi: 10.1002/anie.202210934. PMID:36198083 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA