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| | <StructureSection load='1fp1' size='340' side='right'caption='[[1fp1]], [[Resolution|resolution]] 1.82Å' scene=''> | | <StructureSection load='1fp1' size='340' side='right'caption='[[1fp1]], [[Resolution|resolution]] 1.82Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1fp1]] is a 1 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=1FP1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FP1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1fp1]] is a 1 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=1FP1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FP1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HCC:2,4,4-TRIHYDROXYCHALCONE'>HCC</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HCC:2,4,4-TRIHYDROXYCHALCONE'>HCC</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fp2|1fp2]], [[1fpx|1fpx]], [[1fpq|1fpq]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fp2|1fp2]], [[1fpx|1fpx]], [[1fpq|1fpq]]</div></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=1fp1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fp1 OCA], [http://pdbe.org/1fp1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fp1 RCSB], [http://www.ebi.ac.uk/pdbsum/1fp1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fp1 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=1fp1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fp1 OCA], [https://pdbe.org/1fp1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fp1 RCSB], [https://www.ebi.ac.uk/pdbsum/1fp1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fp1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CHOMT_MEDSA CHOMT_MEDSA]] Methylates the 2'-hydroxyl of isoliquiritigenin and licodione. Does not methylate narigenin chalcone, caffeic acid or daidzein. Involved in the root nodulation initiation by promoting the biosynthesis of nod-inducing molecules.<ref>PMID:1731632</ref> <ref>PMID:9055445</ref> | + | [[https://www.uniprot.org/uniprot/CHOMT_MEDSA CHOMT_MEDSA]] Methylates the 2'-hydroxyl of isoliquiritigenin and licodione. Does not methylate narigenin chalcone, caffeic acid or daidzein. Involved in the root nodulation initiation by promoting the biosynthesis of nod-inducing molecules.<ref>PMID:1731632</ref> <ref>PMID:9055445</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Structural highlights
Function
[CHOMT_MEDSA] Methylates the 2'-hydroxyl of isoliquiritigenin and licodione. Does not methylate narigenin chalcone, caffeic acid or daidzein. Involved in the root nodulation initiation by promoting the biosynthesis of nod-inducing molecules.[1] [2]
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 O-methyltransferase (ChOMT) and isoflavone O-methyltransferase (IOMT) are S-adenosyl-l-methionine (SAM) dependent plant natural product methyltransferases involved in secondary metabolism in Medicago sativa (alfalfa). Here we report the crystal structure of ChOMT in complex with the product S-adenosyl-l-homocysteine and the substrate isoliquiritigenin (4,2',4'-trihydroxychalcone) refined to 1.8 A as well as the crystal structure of IOMT in complex with the products S-adenosyl-l-homocysteine and isoformononetin (4'-hydroxy-7-methoxyisoflavone) refined to 1.4 A. These two OMTs constitute the first plant methyltransferases to be structurally characterized and reveal a novel oligomerization domain and the molecular determinants for substrate selection. As such, this work provides a structural basis for understanding the substrate specificity of the diverse family of plant OMTs and facilitates the engineering of novel activities in this extensive class of natural product biosynthetic enzymes.
Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases.,Zubieta C, He XZ, Dixon RA, Noel JP Nat Struct Biol. 2001 Mar;8(3):271-9. PMID:11224575[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Maxwell CA, Edwards R, Dixon RA. Identification, purification, and characterization of S-adenosyl-L-methionine: isoliquiritigenin 2'-O-methyltransferase from alfalfa (Medicago sativa L.). Arch Biochem Biophys. 1992 Feb 14;293(1):158-66. PMID:1731632
- ↑ Ichimura M, Furuno T, Takahashi T, Dixon RA, Ayabe S. Enzymic O-methylation of isoliquiritigenin and licodione in alfalfa and licorice cultures. Phytochemistry. 1997 Mar;44(6):991-5. PMID:9055445
- ↑ Zubieta C, He XZ, Dixon RA, Noel JP. Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases. Nat Struct Biol. 2001 Mar;8(3):271-9. PMID:11224575 doi:http://dx.doi.org/10.1038/85029
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