3v0s

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==Crystal Structure of Perakine Reductase, Founder Member of a Novel AKR Subfamily with Unique Conformational Changes during NADPH Binding==
==Crystal Structure of Perakine Reductase, Founder Member of a Novel AKR Subfamily with Unique Conformational Changes during NADPH Binding==
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<StructureSection load='3v0s' size='340' side='right' caption='[[3v0s]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
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<StructureSection load='3v0s' size='340' side='right'caption='[[3v0s]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3v0s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Devilpepper Devilpepper]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V0S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3V0S FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3v0s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ophioxylon_serpentinum Ophioxylon serpentinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V0S FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATR:2-MONOPHOSPHOADENOSINE-5-DIPHOSPHATE'>ATR</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATR:2-MONOPHOSPHOADENOSINE-5-DIPHOSPHATE'>ATR</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3v0t|3v0t]], [[3v0u|3v0u]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3v0t|3v0t]], [[3v0u|3v0u]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4060 Devilpepper])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PR ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4060 Ophioxylon serpentinum])</td></tr>
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<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=3v0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v0s OCA], [http://pdbe.org/3v0s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3v0s RCSB], [http://www.ebi.ac.uk/pdbsum/3v0s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3v0s ProSAT]</span></td></tr>
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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=3v0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v0s OCA], [https://pdbe.org/3v0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v0s RCSB], [https://www.ebi.ac.uk/pdbsum/3v0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v0s ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PERR_RAUSE PERR_RAUSE]] Aldo-keto reductase involved in the biosynthesis of monoterpenoid indole alkaloids. Broad substrate specificity enzyme with a high selectivity in the group of alkaloids. Can use perakine, 19(S),20(R)-dihydro-peraksine-17,21-al, cinnamic aldehyde, p-coumaric aldehyde and 3-(3,4,5-trimethoxyphenyl)propanal as substrates, but not ketosteroids such as progesterone. NADPH could not be replaced by NADH.<ref>PMID:18409028</ref>
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[[https://www.uniprot.org/uniprot/PERR_RAUSE PERR_RAUSE]] Aldo-keto reductase involved in the biosynthesis of monoterpenoid indole alkaloids. Broad substrate specificity enzyme with a high selectivity in the group of alkaloids. Can use perakine, 19(S),20(R)-dihydro-peraksine-17,21-al, cinnamic aldehyde, p-coumaric aldehyde and 3-(3,4,5-trimethoxyphenyl)propanal as substrates, but not ketosteroids such as progesterone. NADPH could not be replaced by NADH.<ref>PMID:18409028</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Devilpepper]]
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[[Category: Large Structures]]
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[[Category: Ophioxylon serpentinum]]
[[Category: Chen, Y]]
[[Category: Chen, Y]]
[[Category: Mindnich, R]]
[[Category: Mindnich, R]]

Revision as of 08:21, 20 July 2022

Crystal Structure of Perakine Reductase, Founder Member of a Novel AKR Subfamily with Unique Conformational Changes during NADPH Binding

PDB ID 3v0s

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