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| | <StructureSection load='6dx9' size='340' side='right'caption='[[6dx9]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='6dx9' size='340' side='right'caption='[[6dx9]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6dx9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Common_horsetail Common horsetail]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DX9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DX9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6dx9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Equisetum_arvense Equisetum arvense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DX9 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CHS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3258 Common horsetail])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Naringenin-chalcone_synthase Naringenin-chalcone synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.74 2.3.1.74] </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=6dx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dx9 OCA], [https://pdbe.org/6dx9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dx9 RCSB], [https://www.ebi.ac.uk/pdbsum/6dx9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dx9 ProSAT]</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=6dx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dx9 OCA], [http://pdbe.org/6dx9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dx9 RCSB], [http://www.ebi.ac.uk/pdbsum/6dx9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dx9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CHSY_EQUAR CHSY_EQUAR]] The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin. | + | [https://www.uniprot.org/uniprot/CHSY_EQUAR CHSY_EQUAR] The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6dx9" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6dx9" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Chalcone synthase|Chalcone synthase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Common horsetail]] | + | [[Category: Equisetum arvense]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Naringenin-chalcone synthase]]
| + | [[Category: Chiang YC]] |
| - | [[Category: Chiang, Y C]] | + | [[Category: Liou G]] |
| - | [[Category: Liou, G]] | + | [[Category: Wang Y]] |
| - | [[Category: Wang, Y]] | + | [[Category: Weng JK]] |
| - | [[Category: Weng, J K]] | + | |
| - | [[Category: Flavonoid]]
| + | |
| - | [[Category: Polyketide synthase]]
| + | |
| - | [[Category: Thiolase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
CHSY_EQUAR The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin.
Publication Abstract from PubMed
Flavonoids are important polyphenolic natural products, ubiquitous in land plants, that play diverse functions in plants' survival in their ecological niches, including UV protection, pigmentation for attracting pollinators, symbiotic nitrogen fixation, and defense against herbivores. Chalcone synthase (CHS) catalyzes the first committed step in plant flavonoid biosynthesis and is highly conserved in all land plants. In several previously reported crystal structures of CHSs from flowering plants, the catalytic cysteine is oxidized to sulfinic acid, indicating enhanced nucleophilicity in this residue associated with its increased susceptibility to oxidation. In this study, we report a set of new crystal structures of CHSs representing all five major lineages of land plants (bryophytes, lycophytes, monilophytes, gymnosperms, and angiosperms), spanning 500 million years of evolution. We reveal that the structures of CHS from a lycophyte and a moss species preserve the catalytic cysteine in a reduced state, in contrast to the cysteine sulfinic acid seen in all euphyllophyte CHS structures. In vivo complementation, in vitro biochemical and mutagenesis analyses, and molecular dynamics simulations identified a set of residues that differ between basal-plant and euphyllophyte CHSs and modulate catalytic cysteine reactivity. We propose that the CHS active-site environment has evolved in euphyllophytes to further enhance the nucleophilicity of the catalytic cysteine since the divergence of euphyllophytes from other vascular plant lineages 400 million years ago. These changes in CHS could have contributed to the diversification of flavonoid biosynthesis in euphyllophytes, which in turn contributed to their dominance in terrestrial ecosystems.
Mechanistic basis for the evolution of chalcone synthase catalytic cysteine reactivity in land plants.,Liou G, Chiang YC, Wang Y, Weng JK J Biol Chem. 2018 Oct 5. pii: RA118.005695. doi: 10.1074/jbc.RA118.005695. PMID:30291143[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Liou G, Chiang YC, Wang Y, Weng JK. Mechanistic basis for the evolution of chalcone synthase catalytic cysteine reactivity in land plants. J Biol Chem. 2018 Oct 5. pii: RA118.005695. doi: 10.1074/jbc.RA118.005695. PMID:30291143 doi:http://dx.doi.org/10.1074/jbc.RA118.005695
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