View source for 7cs3


==IiPLR1 with NADP+==
<StructureSection load='7cs3' size='340' side='right'caption='[[7cs3]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7cs3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Isatis_tinctoria Isatis tinctoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CS3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CS3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4002185&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></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=7cs3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cs3 OCA], [https://pdbe.org/7cs3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cs3 RCSB], [https://www.ebi.ac.uk/pdbsum/7cs3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cs3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/I6LRS1_ISATI I6LRS1_ISATI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pinoresinol-lariciresinol reductases (PLRs) are enzymes involved in the lignan biosynthesis after the initial dimerization of two monolignols, and this represents the entry point for the synthesis of 8-8' lignans and contributes greatly to their structural diversity. Of particular interest has been the determination of how differing substrate specificities are achieved with these enzymes. Here, we present crystal structures of IiPLR1 from Isatis indigotica and pinoresinol reductases (PrRs) AtPrR1 and AtPrR2 from Arabidopsis thaliana, in the apo, substrate-bound and product-bound states. Each structure contains a head-to-tail homodimer, and the catalytic pocket comprises structural elements from both monomers. beta4 loop covers the top of the pocket, and residue 98 from the loop governs catalytic specificity. The substrate specificities of IiPLR1 and AtPrR2 can be switched via structure-guided mutagenesis. Our study provides insight into the molecular mechanism underlying the substrate specificity of PLRs/PrRs and suggests an efficient strategy for the large-scale commercial production of the pharmaceutically valuable compound lariciresinol.

Structure-based engineering of substrate specificity for pinoresinol-lariciresinol reductases.,Xiao Y, Shao K, Zhou J, Wang L, Ma X, Wu D, Yang Y, Chen J, Feng J, Qiu S, Lv Z, Zhang L, Zhang P, Chen W Nat Commun. 2021 May 14;12(1):2828. doi: 10.1038/s41467-021-23095-y. PMID:33990581<ref>PMID:33990581</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7cs3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Isatis tinctoria]]
[[Category: Large Structures]]
[[Category: Shao K]]
[[Category: Zhang P]]