8j2z
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Glucosyl transferase== | |
| + | <StructureSection load='8j2z' size='340' side='right'caption='[[8j2z]], [[Resolution|resolution]] 2.78Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8j2z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Nicotiana_tabacum Nicotiana tabacum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8J2Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8J2Z 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]] 2.783Å</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=8j2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8j2z OCA], [https://pdbe.org/8j2z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8j2z RCSB], [https://www.ebi.ac.uk/pdbsum/8j2z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8j2z ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A8K1ZRH3_NICBE A0A8K1ZRH3_NICBE] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Enzymes are essential catalysts in biological systems. Substrate inhibition, once dismissed, is now observed in 20% of enzymes(1) and is attributed to the formation of an unproductive enzyme-substrate complex, with no structural evidence of unproductivity provided to date(1-6). This study uncovers the molecular mechanism of substrate inhibition in tobacco glucosyltransferase NbUGT72AY1, which transfers glucose to phenols for plant protection. The peculiarity that beta-carotene strongly attenuates the substrate inhibition of NbUGT72AY1, despite being a competitive inhibitor, allows to determine the conformational changes that occur during substrate binding in both active and substrate-inhibited complexes. Crystallography reveals structurally different ternary enzyme-substrate complexes that do not conform to classical mechanisms. An alternative pathway suggests substrates bind randomly, but the reaction occurs only if a specific order is followed (asymmetric cooperativity). This unreported paradigm explains substrate inhibition and reactivation by competitive inhibitors, opening new research avenues in metabolic regulation and industrial applications. | ||
| - | + | beta-Carotene alleviates substrate inhibition caused by asymmetric cooperativity.,Liao J, Shahul Hameed UF, Hoffmann TD, Kurze E, Sun G, Steinchen W, Nicoli A, Di Pizio A, Kuttler C, Song C, Catici DAM, Assaad-Gerbert F, Hoffmann T, Arold ST, Schwab WG Nat Commun. 2025 Mar 29;16(1):3065. doi: 10.1038/s41467-025-58259-7. PMID:40157902<ref>PMID:40157902</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8j2z" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Nicotiana tabacum]] | ||
| + | [[Category: Arold ST]] | ||
| + | [[Category: Hameed UFS]] | ||
Current revision
Glucosyl transferase
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