1qyc: Difference between revisions

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<StructureSection load='1qyc' size='340' side='right'caption='[[1qyc]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1qyc' size='340' side='right'caption='[[1qyc]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1qyc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Loblolly_pine Loblolly pine]. 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>
<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>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qyd|1qyd]]</div></td></tr>
</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>
<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>
<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>
</table>
</table>
== Function ==
[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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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<ref>PMID:13129921</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1qyc" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Loblolly pine]]
[[Category: Pinus taeda]]
[[Category: Bedgar, D L]]
[[Category: Bedgar DL]]
[[Category: Davin, L B]]
[[Category: Davin LB]]
[[Category: Gang, D R]]
[[Category: Gang DR]]
[[Category: Halls, S C]]
[[Category: Halls SC]]
[[Category: Hilsenbeck, J L]]
[[Category: Hilsenbeck JL]]
[[Category: Kang, C]]
[[Category: Kang C]]
[[Category: Kasahara, H]]
[[Category: Kasahara H]]
[[Category: Lawrence, P K]]
[[Category: Lawrence PK]]
[[Category: Min, T]]
[[Category: Min T]]
[[Category: Park, H]]
[[Category: Park H]]
[[Category: Youn, B]]
[[Category: Youn B]]
[[Category: Ifr]]
[[Category: Isoflavonoid]]
[[Category: Lignan]]
[[Category: Nadph-dependent aromatic alcohol reductase]]
[[Category: Pcber]]
[[Category: Plant protein]]
[[Category: Plr]]

Latest revision as of 11:18, 14 February 2024

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

Structural highlights

1qyc is a 2 chain structure with sequence from Pinus taeda. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Gang DR, Kasahara H, Xia ZQ, Vander Mijnsbrugge K, Bauw G, Boerjan W, Van Montagu M, Davin LB, Lewis NG. Evolution of plant defense mechanisms. Relationships of phenylcoumaran benzylic ether reductases to pinoresinol-lariciresinol and isoflavone reductases. J Biol Chem. 1999 Mar 12;274(11):7516-27. PMID:10066819 doi:10.1074/jbc.274.11.7516
  2. ↑ Shoji T, Winz R, Iwase T, Nakajima K, Yamada Y, Hashimoto T. Expression patterns of two tobacco isoflavone reductase-like genes and their possible roles in secondary metabolism in tobacco. Plant Mol Biol. 2002 Oct;50(3):427-40. PMID:12369619 doi:10.1023/a:1019867732278

1qyc, resolution 2.20Å

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