7csd | pdb_00007csd

AtPrR1 with NADP+ and (+)lariciresinol

spinqualitylabelsall models 7csd, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7csd is a 4 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7970997Å Ligands: GFU, NDP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PILR1_ARATH Reductase involved in lignan biosynthesis (PubMed:18347017, PubMed:25107662). Involved in secondary cell wall biosynthesis in fiber cells (PubMed:25107662). Unlike conventional pinoresinol reductases that can reduce both pinoresinol and lariciresinol, PRR1 shows a strict substrate preference toward pinoresinol (PubMed:18347017). Active on both (+) and (-)-pinoresinol (PubMed:18347017). Abstracts the 4R-hydride from the NADPH cofactor during catalysis (PubMed:18347017). Publication Abstract from PubMed Pinoresinol-lariciresinol reductases (PLRs) are enzymes involved in the lignan biosynthesis after the initial dimerization of two monolignols, and this represents the entry point for the synthesis of 8-8' lignans and contributes greatly to their structural diversity. Of particular interest has been the determination of how differing substrate specificities are achieved with these enzymes. Here, we present crystal structures of IiPLR1 from Isatis indigotica and pinoresinol reductases (PrRs) AtPrR1 and AtPrR2 from Arabidopsis thaliana, in the apo, substrate-bound and product-bound states. Each structure contains a head-to-tail homodimer, and the catalytic pocket comprises structural elements from both monomers. beta4 loop covers the top of the pocket, and residue 98 from the loop governs catalytic specificity. The substrate specificities of IiPLR1 and AtPrR2 can be switched via structure-guided mutagenesis. Our study provides insight into the molecular mechanism underlying the substrate specificity of PLRs/PrRs and suggests an efficient strategy for the large-scale commercial production of the pharmaceutically valuable compound lariciresinol. Structure-based engineering of substrate specificity for pinoresinol-lariciresinol reductases.,Xiao Y, Shao K, Zhou J, Wang L, Ma X, Wu D, Yang Y, Chen J, Feng J, Qiu S, Lv Z, Zhang L, Zhang P, Chen W Nat Commun. 2021 May 14;12(1):2828. doi: 10.1038/s41467-021-23095-y. PMID:33990581 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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