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| | <StructureSection load='4whm' size='340' side='right'caption='[[4whm]], [[Resolution|resolution]] 1.85Å' scene=''> | | <StructureSection load='4whm' size='340' side='right'caption='[[4whm]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4whm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Butterfly_pea Butterfly pea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WHM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WHM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4whm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clitoria_ternatea Clitoria ternatea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WHM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WHM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wc4|3wc4]], [[4rel|4rel]], [[4rem|4rem]], [[4ren|4ren]]</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=4whm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4whm OCA], [https://pdbe.org/4whm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4whm RCSB], [https://www.ebi.ac.uk/pdbsum/4whm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4whm ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ct3GT-A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=43366 Butterfly pea])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Anthocyanidin_3-O-glucosyltransferase Anthocyanidin 3-O-glucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.115 2.4.1.115] </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=4whm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4whm OCA], [http://pdbe.org/4whm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4whm RCSB], [http://www.ebi.ac.uk/pdbsum/4whm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4whm ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A4F1R4_CLITE A4F1R4_CLITE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Anthocyanidin 3-O-glucosyltransferase]] | + | [[Category: Clitoria ternatea]] |
| - | [[Category: Butterfly pea]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hiromoto, T]] | + | [[Category: Hiromoto T]] |
| - | [[Category: Honjo, E]] | + | [[Category: Honjo E]] |
| - | [[Category: Kuroki, R]] | + | [[Category: Kuroki R]] |
| - | [[Category: Tamada, T]] | + | [[Category: Tamada T]] |
| - | [[Category: Complexed with udp]]
| + | |
| - | [[Category: Ct3gt-a]]
| + | |
| - | [[Category: Gt-b fold]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Ugt78k6]]
| + | |
| Structural highlights
Function
A4F1R4_CLITE
Publication Abstract from PubMed
UDP-glucose: anthocyanidin 3-O-glucosyltransferase (UGT78K6) from Clitoria ternatea catalyzes the transfer of glucose from UDP-glucose to anthocyanidins such as delphinidin. After the acylation of the 3-O-glucosyl residue, the 3'- and 5'-hydroxyl groups of the product are further glucosylated by a glucosyltransferase in the biosynthesis of ternatins, which are anthocyanin pigments. To understand the acceptor-recognition scheme of UGT78K6, the crystal structure of UGT78K6 and its complex forms with anthocyanidin delphinidin and petunidin, and flavonol kaempferol were determined to resolutions of 1.85 A, 2.55 A, 2.70 A, and 1.75 A, respectively. The enzyme recognition of unstable anthocyanidin aglycones was initially observed in this structural determination. The anthocyanidin- and flavonol-acceptor binding details are almost identical in each complex structure, although the glucosylation activities against each acceptor were significantly different. The 3-hydroxyl groups of the acceptor substrates were located at hydrogen-bonding distances to the Nepsilon2 atom of the His17 catalytic residue, supporting a role for glucosyl transfer to the 3-hydroxyl groups of anthocyanidins and flavonols. However, the molecular orientations of these three acceptors are different from those of the known flavonoid glycosyltransferases, VvGT1 and UGT78G1. The acceptor substrates in UGT78K6 are reversely bound to its binding site by a 180 degrees rotation about the O1-O3 axis of the flavonoid backbones observed in VvGT1 and UGT78G1; consequently, the 5- and 7-hydroxyl groups are protected from glucosylation. These substrate recognition schemes are useful to understand the unique reaction mechanism of UGT78K6 for the ternatin biosynthesis, and suggest the potential for controlled synthesis of natural pigments. This article is protected by copyright. All rights reserved.
Structural basis for acceptor-substrate recognition of UDP-glucose: Anthocyanidin 3-O-glucosyltransferase from Clitoria ternatea.,Hiromoto T, Honjo E, Tamada T, Noda N, Kazuma K, Suzuki M, Blaber M, Kuroki R Protein Sci. 2014 Dec 30. doi: 10.1002/pro.2630. PMID:25556637[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hiromoto T, Honjo E, Tamada T, Noda N, Kazuma K, Suzuki M, Blaber M, Kuroki R. Structural basis for acceptor-substrate recognition of UDP-glucose: Anthocyanidin 3-O-glucosyltransferase from Clitoria ternatea. Protein Sci. 2014 Dec 30. doi: 10.1002/pro.2630. PMID:25556637 doi:http://dx.doi.org/10.1002/pro.2630
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