5u6n
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of UDP-glucosyltransferase, UGT74F2 (T15S), with UDP and salicylic acid== | |
| + | <StructureSection load='5u6n' size='340' side='right' caption='[[5u6n]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5u6n]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U6N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5U6N FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GLN:GLUTAMINE'>GLN</scene>, <scene name='pdbligand=LB2:3-O-BETA-D-GLUCOPYRANOSYL-BETA-D-GLUCOPYRANOSE'>LB2</scene>, <scene name='pdbligand=SAL:2-HYDROXYBENZOIC+ACID'>SAL</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">[[5u6s|5u6s]], [[5u6m|5u6m]]</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=5u6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u6n OCA], [http://pdbe.org/5u6n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5u6n RCSB], [http://www.ebi.ac.uk/pdbsum/5u6n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5u6n ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/U74F2_ARATH U74F2_ARATH]] Glycosyltransferase that glucosylates benzoic acid and derivatives. Substrate preference is benzoic acid > salicylic acid (SA) > 3-hydroxybenzoic acid > 4-hydroxybenzoic acid. Catalyzes the formation of both SA 2-O-beta-D-glucoside (SAG) and SA glucose ester (SGE). Has high affinity for the tryptophan precursor anthranilate. Catalyzes the formation of anthranilate glucose ester. Is the major source of this activity in the plant.<ref>PMID:11641410</ref> <ref>PMID:12475971</ref> <ref>PMID:17085977</ref> <ref>PMID:18226820</ref> <ref>PMID:18385129</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Salicylic acid (SA) is a signaling molecule utilized by plants in response to various stresses. Through conjugation with small organic molecules such as glucose, an inactive form of SA is generated which can be transported into and stored in plant vacuoles. In the model organism Arabidopsis thaliana, SA glucose conjugates are formed by two homologous enzymes (UGT74F1 and UGT74F2) that transfer glucose from UDP-glucose to SA. Despite being 77% identical and with conserved active site residues, these enzymes catalyze the formation of different products: UGT74F1 forms salicylic acid glucoside (SAG), while UGT74F2 forms primarily salicylic acid glucose ester (SGE). The position of the glucose on the aglycone determines how SA is stored, further metabolized, and contributes to a defense response. We determined the crystal structures of the UGT74F2 wild-type and T15S mutant enzymes, in different substrate/product complexes. On the basis of the crystal structures and the effect on enzyme activity of mutations in the SA binding site, we propose the catalytic mechanism of SGE and SAG formation and that SA binds to the active site in two conformations, with each enzyme selecting a certain binding mode of SA. Additionally, we show that two threonines are key determinants of product specificity. | ||
| - | + | Differences in salicylic acid glucose conjugations by UGT74F1 and UGT74F2 from Arabidopsis thaliana.,George Thompson AM, Iancu CV, Neet KE, Dean JV, Choe JY Sci Rep. 2017 Apr 20;7:46629. doi: 10.1038/srep46629. PMID:28425481<ref>PMID:28425481</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5u6n" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Choe, J]] | [[Category: Choe, J]] | ||
| - | [[Category: Dean, J | + | [[Category: Dean, J V]] |
| - | [[Category: | + | [[Category: Iancu, C V]] |
| + | [[Category: Thompson, A M.George]] | ||
| + | [[Category: Salicylic acid]] | ||
| + | [[Category: Salicylic acid ester]] | ||
| + | [[Category: Salicylic acid glucoside]] | ||
| + | [[Category: Transferase]] | ||
| + | [[Category: Udp-glucosyltransferase]] | ||
Revision as of 13:01, 4 May 2017
Crystal structure of UDP-glucosyltransferase, UGT74F2 (T15S), with UDP and salicylic acid
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