View source for 7csg


==AtPrR2 in apo form==
<StructureSection load='7csg' size='340' side='right'caption='[[7csg]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7csg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CSG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CSG 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]] 1.9968939&#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=7csg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7csg OCA], [https://pdbe.org/7csg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7csg RCSB], [https://www.ebi.ac.uk/pdbsum/7csg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7csg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PILR2_ARATH PILR2_ARATH] Reductase involved in lignan biosynthesis (PubMed:18347017). Unlike conventional pinoresinol reductases that can reduce both pinoresinol and lariciresinol, PRR2 shows a strict substrate selectivity for (-)-pinoresinol (PubMed:18347017). No activity with (+)-pinoresinol or lariciresinol (PubMed:18347017). Abstracts the 4R-hydride from the NADPH cofactor during catalysis (PubMed:18347017).<ref>PMID:18347017</ref> 
<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 7csg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Shao K]]
[[Category: Zhang P]]