3o26

The structure of salutaridine reductase from Papaver somniferum.

spinqualitylabelsall models 3o26, resolution 1.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3o26 is a 1 chain structure with sequence from Papaver somniferum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.91Å Ligands: NDP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SALR_PAPSO Short-chain dehydrogenases/reductases involved in biosynthesis of morphinan-type benzylisoquinoline and opiate alkaloids natural products (PubMed:22098111). Catalyzes specifically the stereospecific conversion of salutaridine to salutaridinol (PubMed:22098111). Publication Abstract from PubMed The opium poppy (Papaver somniferum L.) is one of the oldest known medicinal plants. In the biosynthetic pathway for morphine and codeine, salutaridine is reduced to salutaridinol by salutaridine reductase (SalR; EC 1.1.1.248) using NADPH as coenzyme. Here we report the atomic structure of SalR to a resolution of ~1.9A in the presence of NADPH. The core structure is highly homologous to the other members of the short chain dehydrogenase/reductase (SDR) family. The major difference is that the nicotinamide moiety and the substrate-binding pocket are covered by a loop (residues 265-279) and on top of that lies a large 'flap' like domain (residues 105-140). This configuration appears to be a combination of the two common structural themes found in other members of the SDR family. Previous modeling studies suggested that substrate inhibition is due mutually exclusive productive and nonproductive modes of substrate binding in the active site. This model was tested via site-directed mutagenesis and a number of these mutations abrogated substrate inhibition. However, the atomic structure of SalR shows that these mutated residues are, instead, distributed over a wide area of the enzyme and many are not in the active site. To explain how residues distal to the active site might affect catalysis, a model is presented whereby SalR may undergo significant conformational changes during catalytic turnover. The atomic structure of salutaridine reductase from the opium poppy Papaver somniferum.,Higashi Y, Kutchan TM, Smith TJ J Biol Chem. 2010 Dec 17. PMID:21169353 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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