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1qyd

From Proteopedia

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[[Image:1qyd.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= 1qyd |SIZE=350|CAPTION= <scene name='initialview01'>1qyd</scene>, resolution 2.5&Aring;
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<StructureSection load='1qyd' size='340' side='right'caption='[[1qyd]], [[Resolution|resolution]] 2.50&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'>[[1qyd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thuja_plicata Thuja plicata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QYD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QYD 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]] 2.5&#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=1qyd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qyd OCA], [https://pdbe.org/1qyd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qyd RCSB], [https://www.ebi.ac.uk/pdbsum/1qyd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qyd 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/PILR1_THUPL 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.<ref>PMID:9872995</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/1qyd_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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1QYD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thuja_plicata Thuja plicata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QYD 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=1qyd 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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[[Category: Single protein]]
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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: Thuja plicata]]
[[Category: Thuja plicata]]
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[[Category: Bedgar, D L.]]
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[[Category: Bedgar DL]]
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[[Category: Davin, L B.]]
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[[Category: Davin LB]]
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[[Category: Gang, D R.]]
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[[Category: Gang DR]]
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[[Category: Halls, S C.]]
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[[Category: Halls SC]]
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[[Category: Hilsenbeck, J L.]]
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[[Category: Hilsenbeck JL]]
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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, P K.]]
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[[Category: Lawrence PK]]
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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 1qyd

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