8yj4

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Current revision (09:04, 22 October 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 8yj4 is ON HOLD until Paper Publication
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==The complex structure of SdnG with its analogue of substrate==
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<StructureSection load='8yj4' size='340' side='right'caption='[[8yj4]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8yj4]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Sordaria_araneosa Sordaria araneosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8YJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8YJ4 FirstGlance]. <br>
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</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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1LYT:(5~{R})-5-methyl-5-[[(1~{R},2~{R},5~{R})-2-methyl-5-[(2~{R})-1-oxidanylidenepropan-2-yl]cyclopentyl]methyl]-2-propan-2-yl-cyclopenta-1,3-diene-1-carboxylic+acid'>A1LYT</scene></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=8yj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8yj4 OCA], [https://pdbe.org/8yj4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8yj4 RCSB], [https://www.ebi.ac.uk/pdbsum/8yj4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8yj4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SDNG_SORAA SDNG_SORAA]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Iminium-catalyzed cycloaddition is one of the most prominent examples of organocatalysis, yet a biological counterpart has not been reported despite the wide-spread occurrence of iminium adducts in enzymes. Here, we present biochemical, structural, and computational evidence for iminium catalysis by the natural Diels-Alderase SdnG that catalyzes norbornene formation in sordarin biosynthesis. A Schiff base adduct between the epsilon-nitrogen of active site K127 and the aldehyde group of the enal dienophile was revealed by structural analysis and captured under catalytic conditions via borohydride reduction. This Schiff base adduct positions the substrate into near-attack conformation and decreases the transition state barrier of Diels-Alder cyclization by 8.3 kcal/mol via dienophile activation. A hydrogen bond network consisting of a catalytic triad is proposed to facilitate proton transfer required for iminium formation. This work establishes a new mode of catalysis for Diels-Alderases and points the way to the design of novel iminium based (bio)catalysts.
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Authors:
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Iminium Catalysis in Natural Diels-Alderase.,Sun Z, Zang X, Zhou Q, Ohashi M, Houk KN, Zhou J, Tang Y Nat Catal. 2025 Mar;8(3):218-228. doi: 10.1038/s41929-025-01294-w. Epub 2025 Feb , 6. PMID:40881614<ref>PMID:40881614</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 8yj4" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Sordaria araneosa]]
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[[Category: Yi T]]
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[[Category: Zang X]]
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[[Category: Zhou J]]

Current revision

The complex structure of SdnG with its analogue of substrate

PDB ID 8yj4

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