8ea2
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of 2-hydroxyisoflavanone dehydratase from Pueraria lobate== | |
| + | <StructureSection load='8ea2' size='340' side='right'caption='[[8ea2]], [[Resolution|resolution]] 2.39Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8ea2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pueraria_montana_var._lobata Pueraria montana var. lobata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8EA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EA2 FirstGlance]. <br> | ||
| + | </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=8ea2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ea2 OCA], [https://pdbe.org/8ea2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ea2 RCSB], [https://www.ebi.ac.uk/pdbsum/8ea2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ea2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/E9M5G1_PUEML E9M5G1_PUEML] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Isoflavonoids play important roles in plant defense and also exhibit a range of mammalian health-promoting activities. Their biosynthesis is initiated by two enzymes with unusual catalytic activities; 2-hydroxyisoflavanone synthase (2-HIS), a membrane-bound cytochrome P450 catalyzing a coupled aryl-ring migration and hydroxylation, and 2-hydroxyisoflavanone dehydratase (2-HID), a member of a large carboxylesterase family that paradoxically catalyzes dehydration of 2-hydroxyisoflavanones to isoflavone. Here we report the crystal structures of 2-HIS from Medicago truncatula and 2-HID from Pueraria lobata. The 2-HIS structure reveals a unique cytochrome P450 conformation and heme and substrate binding mode that facilitate the coupled aryl-ring migration and hydroxylation reactions. The 2-HID structure reveals the active site architecture and putative catalytic residues for the dual dehydratase and carboxylesterase activities. Mutagenesis studies revealed key residues involved in substrate binding and specificity. Understanding the structural basis of isoflavone biosynthesis will facilitate the engineering of new bioactive isoflavonoids. | ||
| - | + | The protein conformational basis of isoflavone biosynthesis.,Wang X, Pan H, Sagurthi S, Paris V, Zhuo C, Dixon RA Commun Biol. 2022 Nov 15;5(1):1249. doi: 10.1038/s42003-022-04222-x. PMID:36376429<ref>PMID:36376429</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Pan | + | <div class="pdbe-citations 8ea2" style="background-color:#fffaf0;"></div> |
| - | [[Category: Wang | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pueraria montana var. lobata]] | ||
| + | [[Category: Pan H]] | ||
| + | [[Category: Wang X]] | ||
Revision as of 10:47, 30 November 2022
Structure of 2-hydroxyisoflavanone dehydratase from Pueraria lobate
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