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| | <StructureSection load='1eyp' size='340' side='right'caption='[[1eyp]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='1eyp' size='340' side='right'caption='[[1eyp]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1eyp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Alfalfa Alfalfa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EYP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EYP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1eyp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Alfalfa Alfalfa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EYP FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1eyq|1eyq]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1eyq|1eyq]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chalcone_isomerase Chalcone isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.5.1.6 5.5.1.6] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Chalcone_isomerase Chalcone isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.5.1.6 5.5.1.6] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eyp OCA], [http://pdbe.org/1eyp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1eyp RCSB], [http://www.ebi.ac.uk/pdbsum/1eyp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1eyp ProSAT]</span></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=1eyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eyp OCA], [https://pdbe.org/1eyp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eyp RCSB], [https://www.ebi.ac.uk/pdbsum/1eyp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eyp ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CFI1_MEDSA CFI1_MEDSA]] Catalyzes the intramolecular cyclization of bicyclic chalcones into tricyclic (S)-flavanones. Responsible for the isomerization of 4,2',4',6'-tetrahydroxychalcone (also termed chalcone) into naringenin.<ref>PMID:10966651</ref> <ref>PMID:11955065</ref> <ref>PMID:11698411</ref> | + | [[https://www.uniprot.org/uniprot/CFI1_MEDSA CFI1_MEDSA]] Catalyzes the intramolecular cyclization of bicyclic chalcones into tricyclic (S)-flavanones. Responsible for the isomerization of 4,2',4',6'-tetrahydroxychalcone (also termed chalcone) into naringenin.<ref>PMID:10966651</ref> <ref>PMID:11955065</ref> <ref>PMID:11698411</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Structural highlights
Function
[CFI1_MEDSA] Catalyzes the intramolecular cyclization of bicyclic chalcones into tricyclic (S)-flavanones. Responsible for the isomerization of 4,2',4',6'-tetrahydroxychalcone (also termed chalcone) into naringenin.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Chalcone isomerase (CHI) catalyzes the intramolecular cyclization of chalcone synthesized by chalcone synthase (CHS) into (2S)-naringenin, an essential compound in the biosynthesis of anthocyanin pigments, inducers of Rhizobium nodulation genes, and antimicrobial phytoalexins. The 1.85 A resolution crystal structure of alfalfa CHI in complex with (2S)-naringenin reveals a novel open-faced beta-sandwich fold. Currently, proteins with homologous primary sequences are found only in higher plants. The topology of the active site cleft defines the stereochemistry of the cyclization reaction. The structure and mutational analysis suggest a mechanism in which shape complementarity of the binding cleft locks the substrate into a constrained conformation that allows the reaction to proceed with a second-order rate constant approaching the diffusion controlled limit. This structure raises questions about the evolutionary history of this structurally unique plant enzyme.
Structure and mechanism of the evolutionarily unique plant enzyme chalcone isomerase.,Jez JM, Bowman ME, Dixon RA, Noel JP Nat Struct Biol. 2000 Sep;7(9):786-91. PMID:10966651[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jez JM, Bowman ME, Dixon RA, Noel JP. Structure and mechanism of the evolutionarily unique plant enzyme chalcone isomerase. Nat Struct Biol. 2000 Sep;7(9):786-91. PMID:10966651 doi:10.1038/79025
- ↑ Jez JM, Bowman ME, Noel JP. Role of hydrogen bonds in the reaction mechanism of chalcone isomerase. Biochemistry. 2002 Apr 23;41(16):5168-76. PMID:11955065
- ↑ Jez JM, Noel JP. Reaction mechanism of chalcone isomerase. pH dependence, diffusion control, and product binding differences. J Biol Chem. 2002 Jan 11;277(2):1361-9. Epub 2001 Nov 6. PMID:11698411 doi:10.1074/jbc.M109224200
- ↑ Jez JM, Bowman ME, Dixon RA, Noel JP. Structure and mechanism of the evolutionarily unique plant enzyme chalcone isomerase. Nat Struct Biol. 2000 Sep;7(9):786-91. PMID:10966651 doi:10.1038/79025
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