2p4h: Difference between revisions

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==Crystal Structure of Vestitone Reductase from Alfalfa (Medicago sativa L.)==
==Crystal Structure of Vestitone Reductase from Alfalfa (Medicago sativa L.)==
<StructureSection load='2p4h' size='340' side='right' caption='[[2p4h]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
<StructureSection load='2p4h' size='340' side='right'caption='[[2p4h]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2p4h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Alfalfa Alfalfa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P4H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2P4H FirstGlance]. <br>
<table><tr><td colspan='2'>[[2p4h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Medicago_sativa Medicago sativa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P4H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P4H FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Vestitone Reductase ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3879 Alfalfa])</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]] 1.4&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2p4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p4h OCA], [http://pdbe.org/2p4h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2p4h RCSB], [http://www.ebi.ac.uk/pdbsum/2p4h PDBsum]</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=2p4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p4h OCA], [https://pdbe.org/2p4h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p4h RCSB], [https://www.ebi.ac.uk/pdbsum/2p4h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p4h ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/VESTR_MEDSA VESTR_MEDSA]] Stereospecific enzyme that catalyzes the NADPH-dependent reduction of (3R)-vestitone to (3R,4R)-4'-methoxyisoflavan-2',4,7-triol (DMI). Has no activity with (3S)-vestitone. Catalyzes the penultimate step in the biosynthesis of the phytoalexin medicarpin, and thereby contributes to plant defense reactions.<ref>PMID:7625843</ref> <ref>PMID:7805842</ref> <ref>PMID:8071365</ref>
[https://www.uniprot.org/uniprot/VESTR_MEDSA VESTR_MEDSA] Stereospecific enzyme that catalyzes the NADPH-dependent reduction of (3R)-vestitone to (3R,4R)-4'-methoxyisoflavan-2',4,7-triol (DMI). Has no activity with (3S)-vestitone. Catalyzes the penultimate step in the biosynthesis of the phytoalexin medicarpin, and thereby contributes to plant defense reactions.<ref>PMID:7625843</ref> <ref>PMID:7805842</ref> <ref>PMID:8071365</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p4/2p4h_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p4/2p4h_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata 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=2p4h ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Isoflavonoids are commonly found in leguminous plants, where they play important roles in plant defense and have significant health benefits for animals and humans. Vestitone reductase catalyzes a stereospecific NADPH-dependent reduction of (3R)-vestitone in the biosynthesis of the antimicrobial isoflavonoid phytoalexin medicarpin. The crystal structure of alfalfa (Medicago sativa L.) vestitone reductase has been determined at 1.4 A resolution. The structure contains a classic Rossmann fold domain in the N terminus and a small C-terminal domain. Sequence and structural analysis showed that vestitone reductase is a member of the short-chain dehydrogenase/reductase (SDR) superfamily despite the low levels of sequence identity, and the prominent structural differences from other SDR enzymes with known structures. The putative binding sites for the co-factor NADPH and the substrate (3R)-vestitone were defined and located in a large cleft formed between the N and C-terminal domains of enzyme. Potential key residues for enzyme activity were also identified, including the catalytic triad Ser129-Tyr164-Lys168. A molecular docking study showed that (3R)-vestitone, but not the (3S) isomer, forms favored interactions with the co-factor and catalytic triad, thus providing an explanation for the enzyme's strict substrate stereo-specificity.
Crystal structure of vestitone reductase from alfalfa (Medicago sativa L.).,Shao H, Dixon RA, Wang X J Mol Biol. 2007 May 25;369(1):265-76. Epub 2007 Mar 21. PMID:17433362<ref>PMID:17433362</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2p4h" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Alfalfa]]
[[Category: Large Structures]]
[[Category: Dixon, R A]]
[[Category: Medicago sativa]]
[[Category: Shao, H]]
[[Category: Dixon RA]]
[[Category: Wang, X]]
[[Category: Shao H]]
[[Category: Isoflavonoid]]
[[Category: Wang X]]
[[Category: Nadph-dependent reductase]]
[[Category: Plant protein]]
Retrieved from "https://proteopedia.org/2p4h"