2pq6: Difference between revisions
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==Crystal structure of Medicago truncatula UGT85H2- Insights into the structural basis of a multifunctional (Iso) flavonoid glycosyltransferase== | ==Crystal structure of Medicago truncatula UGT85H2- Insights into the structural basis of a multifunctional (Iso) flavonoid glycosyltransferase== | ||
<StructureSection load='2pq6' size='340' side='right' caption='[[2pq6]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='2pq6' size='340' side='right'caption='[[2pq6]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2pq6]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2pq6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Medicago_truncatula Medicago truncatula]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PQ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PQ6 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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=2pq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pq6 OCA], [https://pdbe.org/2pq6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pq6 RCSB], [https://www.ebi.ac.uk/pdbsum/2pq6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pq6 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A6XNC5_MEDTR A6XNC5_MEDTR] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pq/2pq6_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pq/2pq6_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2pq6 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 26: | Line 30: | ||
==See Also== | ==See Also== | ||
*[[Glycosyltransferase|Glycosyltransferase]] | *[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Escamilla-Trevino | [[Category: Medicago truncatula]] | ||
[[Category: Li | [[Category: Escamilla-Trevino LL]] | ||
[[Category: Modolo | [[Category: Li L]] | ||
[[Category: Wang | [[Category: Modolo LV]] | ||
[[Category: Wang X]] | |||
Latest revision as of 14:06, 30 August 2023
Crystal structure of Medicago truncatula UGT85H2- Insights into the structural basis of a multifunctional (Iso) flavonoid glycosyltransferaseCrystal structure of Medicago truncatula UGT85H2- Insights into the structural basis of a multifunctional (Iso) flavonoid glycosyltransferase
Structural highlights
FunctionEvolutionary 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(Iso)flavonoids are a diverse group of plant secondary metabolites with important effects on plant, animal and human health. They exist in various glycosidic forms. Glycosylation, which may determine their bioactivities and functions, is controlled by specific plant uridine diphosphate glycosyltransferases (UGTs). We describe a new multifunctional (iso)flavonoid glycosyltransferase, UGT85H2, from the model legume Medicago truncatula with activity towards a number of phenylpropanoid-derived natural products including the flavonol kaempferol, the isoflavone biochanin A, and the chalcone isoliquiritigenin. The crystal structure of UGT85H2 has been determined at 2.1 A resolution, and reveals distinct structural features that are different from those of other UGTs and related to the enzyme's functions and substrate specificities. Structural and comparative analyses revealed the putative binding sites for the donor and acceptor substrates that are located in a large cleft formed between the two domains of the enzyme, and indicated that Trp360 may undergo a conformational change after sugar donor binding to the enzyme. UGT85H2 has higher specificity for flavonol than for isoflavone. Further substrate docking combined with enzyme activity assay and kinetic analysis provided structural insights into this substrate specificity and preference. Crystal structure of Medicago truncatula UGT85H2--insights into the structural basis of a multifunctional (iso)flavonoid glycosyltransferase.,Li L, Modolo LV, Escamilla-Trevino LL, Achnine L, Dixon RA, Wang X J Mol Biol. 2007 Jul 27;370(5):951-63. Epub 2007 May 18. PMID:17553523[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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