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1qyc

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[[Image:1qyc.gif|left|200px]]
 
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{{Structure
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==Crystal structures of pinoresinol-lariciresinol and phenylcoumaran benzylic ether reductases, and their relationship to isoflavone reductases==
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|PDB= 1qyc |SIZE=350|CAPTION= <scene name='initialview01'>1qyc</scene>, resolution 2.2&Aring;
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<StructureSection load='1qyc' size='340' side='right'caption='[[1qyc]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1qyc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pinus_taeda Pinus taeda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QYC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QYC FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qyc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qyc OCA], [https://pdbe.org/1qyc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qyc RCSB], [https://www.ebi.ac.uk/pdbsum/1qyc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qyc ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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'''Crystal structures of pinoresinol-lariciresinol and phenylcoumaran benzylic ether reductases, and their relationship to isoflavone reductases'''
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[https://www.uniprot.org/uniprot/PCBER_PINTA PCBER_PINTA] Oxidoreductase involved in lignan biosynthesis. Catalyzes the NADPH-dependent reduction of phenylcoumaran benzylic ethers. Converts dehydrodiconiferyl alcohol (DDC) to isodihydrodehydrodiconiferyl alcohol (IDDDC), and dihydrodehydrodiconiferyl alcohol (DDDC) to tetrahydrodehydrodiconiferyl alcohol (TDDC).<ref>PMID:10066819</ref> <ref>PMID:12369619</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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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.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qy/1qyc_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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1QYC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pinus_taeda Pinus taeda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QYC OCA].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qyc ConSurf].
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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:[http://www.ncbi.nlm.nih.gov/pubmed/13129921 13129921]
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Pinus taeda]]
[[Category: Pinus taeda]]
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[[Category: Single protein]]
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[[Category: Bedgar DL]]
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[[Category: Bedgar, D L.]]
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[[Category: Davin LB]]
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[[Category: Davin, L B.]]
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[[Category: Gang DR]]
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[[Category: Gang, D R.]]
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[[Category: Halls SC]]
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[[Category: Halls, S C.]]
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[[Category: Hilsenbeck JL]]
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[[Category: Hilsenbeck, J L.]]
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[[Category: Kang C]]
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[[Category: Kang, C.]]
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[[Category: Kasahara H]]
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[[Category: Kasahara, H.]]
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[[Category: Lawrence PK]]
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[[Category: Lawrence, P K.]]
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[[Category: Min T]]
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[[Category: Min, T.]]
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[[Category: Park H]]
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[[Category: Park, H.]]
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[[Category: Youn B]]
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[[Category: Youn, B.]]
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[[Category: ifr]]
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[[Category: isoflavonoid]]
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[[Category: lignan]]
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[[Category: nadph-dependent aromatic alcohol reductase]]
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[[Category: pcber]]
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[[Category: plr]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:44:22 2008''
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Current revision

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

PDB ID 1qyc

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