1qyd

Crystal structures of pinoresinol-lariciresinol and phenylcoumaran benzylic ether reductases, and their relationship to isoflavone reductases

spinqualitylabelsall models 1qyd, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1qyd is a 4 chain structure with sequence from Giant arborvitae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1qyc Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [PILR1_THUPL] Reductase involved in lignan biosynthesis. Catalyzes the enantioselective sequential conversion of (-)-pinoresinol into (-)-lariciresinol and of (-)-lariciresinol into (+)-secoisolariciresinol. Can also convert with a lower efficiency (+)-pinoresinol into (+)-lariciresinol, but not (+)-lariciresinol into (-)-secoisolariciresinol. Abstracts the 4R-hydride from the NADPH cofactor during catalysis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Despite the importance of plant lignans and isoflavonoids in human health protection (e.g. for both treatment and prevention of onset of various cancers) as well as in plant biology (e.g. in defense functions and in heartwood development), systematic studies on the enzymes involved in their biosynthesis have only recently begun. In this investigation, three NADPH-dependent aromatic alcohol reductases were comprehensively studied, namely pinoresinol-lariciresinol reductase (PLR), phenylcoumaran benzylic ether reductase (PCBER), and isoflavone reductase (IFR), which are involved in central steps to the various important bioactive lignans and isoflavonoids. Of particular interest was in determining how differing regio- and enantiospecificities are achieved with the different enzymes, despite each apparently going through similar enone intermediates. Initially, the three-dimensional x-ray crystal structures of both PLR_Tp1 and PCBER_Pt1 were solved and refined to 2.5 and 2.2 A resolutions, respectively. Not only do they share high gene sequence similarity, but their structures are similar, having a continuous alpha/beta NADPH-binding domain and a smaller substrate-binding domain. IFR (whose crystal structure is not yet obtained) was also compared (modeled) with PLR and PCBER and was deduced to have the same overall basic structure. The basis for the distinct enantio-specific and regio-specific reactions of PCBER, PLR, and IFR, as well as the reaction mechanism and participating residues involved (as identified by site-directed mutagenesis), are discussed. Crystal structures of pinoresinol-lariciresinol and phenylcoumaran benzylic ether reductases and their relationship to isoflavone reductases.,Min T, Kasahara H, Bedgar DL, Youn B, Lawrence PK, Gang DR, Halls SC, Park H, Hilsenbeck JL, Davin LB, Lewis NG, Kang C J Biol Chem. 2003 Dec 12;278(50):50714-23. Epub 2003 Sep 16. PMID:13129921 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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