5u6s: Difference between revisions

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<StructureSection load='5u6s' size='340' side='right'caption='[[5u6s]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='5u6s' size='340' side='right'caption='[[5u6s]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5u6s]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U6S OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5U6S FirstGlance]. <br>
<table><tr><td colspan='2'>[[5u6s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U6S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5U6S FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7WV:2-BROMOBENZOIC+ACID'>7WV</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</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]] 1.996&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5u6n|5u6n]], [[5u6m|5u6m]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7WV:2-BROMOBENZOIC+ACID'>7WV</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=PRD_900024:beta-laminaribiose'>PRD_900024</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UGT74F2, GT, SAGT1, SGT1, At2g43820, F18O19.7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=5u6s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u6s OCA], [https://pdbe.org/5u6s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5u6s RCSB], [https://www.ebi.ac.uk/pdbsum/5u6s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5u6s ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5u6s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u6s OCA], [http://pdbe.org/5u6s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5u6s RCSB], [http://www.ebi.ac.uk/pdbsum/5u6s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5u6s ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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> 
[https://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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5u6s" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Arath]]
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Choe, J]]
[[Category: Choe J]]
[[Category: Dean, J V]]
[[Category: Dean JV]]
[[Category: Iancu, C V]]
[[Category: George Thompson AM]]
[[Category: Thompson, A M.George]]
[[Category: Iancu CV]]
[[Category: Salicylic acid]]
[[Category: Salicylic acid glucose ester]]
[[Category: Salicylic acid glucoside]]
[[Category: Transferase]]
[[Category: Udp-glucosyltransferase]]

Latest revision as of 15:45, 6 March 2024

Crystal structure of UDP-glucosyltransferase, UGT74F2, with UDP and 2-bromobenzoic acid

5u6s, resolution 2.00Å

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