|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of UDP-glucosyltransferase, UGT74F2 (T15A), with UDP and 2-bromobenzoic acid== | | ==Crystal structure of UDP-glucosyltransferase, UGT74F2 (T15A), with UDP and 2-bromobenzoic acid== |
| - | <StructureSection load='5v2k' size='340' side='right' caption='[[5v2k]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='5v2k' size='340' side='right'caption='[[5v2k]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5v2k]] 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=5V2K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V2K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5v2k]] 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=5V2K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V2K FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7WV:2-BROMOBENZOIC+ACID'>7WV</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=LB2:3-O-BETA-D-GLUCOPYRANOSYL-BETA-D-GLUCOPYRANOSE'>LB2</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]] 2.002Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5v2j|5v2j]]</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=5v2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v2k OCA], [https://pdbe.org/5v2k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v2k RCSB], [https://www.ebi.ac.uk/pdbsum/5v2k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v2k ProSAT]</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=5v2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v2k OCA], [http://pdbe.org/5v2k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v2k RCSB], [http://www.ebi.ac.uk/pdbsum/5v2k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v2k 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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 20: |
Line 19: |
| | </div> | | </div> |
| | <div class="pdbe-citations 5v2k" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5v2k" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Choe, J]] | + | [[Category: Large Structures]] |
| - | [[Category: Dean, J V]] | + | [[Category: Choe J]] |
| - | [[Category: Iancu, C V]] | + | [[Category: Dean JV]] |
| - | [[Category: Thompson, A M.George]] | + | [[Category: George Thompson AM]] |
| - | [[Category: Salicylic acid]] | + | [[Category: Iancu CV]] |
| - | [[Category: Salicylic acid glucose ester]]
| + | |
| - | [[Category: Salicylic acid glucoside]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Udp-glucosyltransferase]]
| + | |
| Structural highlights
Function
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.[1] [2] [3] [4] [5]
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[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lim EK, Doucet CJ, Li Y, Elias L, Worrall D, Spencer SP, Ross J, Bowles DJ. The activity of Arabidopsis glycosyltransferases toward salicylic acid, 4-hydroxybenzoic acid, and other benzoates. J Biol Chem. 2002 Jan 4;277(1):586-92. Epub 2001 Oct 18. PMID:11641410 doi:http://dx.doi.org/10.1074/jbc.M109287200
- ↑ Quiel JA, Bender J. Glucose conjugation of anthranilate by the Arabidopsis UGT74F2 glucosyltransferase is required for tryptophan mutant blue fluorescence. J Biol Chem. 2003 Feb 21;278(8):6275-81. Epub 2002 Dec 9. PMID:12475971 doi:http://dx.doi.org/10.1074/jbc.M211822200
- ↑ Song JT. Induction of a salicylic acid glucosyltransferase, AtSGT1, is an early disease response in Arabidopsis thaliana. Mol Cells. 2006 Oct 31;22(2):233-8. PMID:17085977
- ↑ Song JT, Koo YJ, Seo HS, Kim MC, Choi YD, Kim JH. Overexpression of AtSGT1, an Arabidopsis salicylic acid glucosyltransferase, leads to increased susceptibility to Pseudomonas syringae. Phytochemistry. 2008 Mar;69(5):1128-34. doi: 10.1016/j.phytochem.2007.12.010., Epub 2008 Jan 28. PMID:18226820 doi:http://dx.doi.org/10.1016/j.phytochem.2007.12.010
- ↑ Eudes A, Bozzo GG, Waller JC, Naponelli V, Lim EK, Bowles DJ, Gregory JF 3rd, Hanson AD. Metabolism of the folate precursor p-aminobenzoate in plants: glucose ester formation and vacuolar storage. J Biol Chem. 2008 May 30;283(22):15451-9. doi: 10.1074/jbc.M709591200. Epub 2008 , Apr 2. PMID:18385129 doi:http://dx.doi.org/10.1074/jbc.M709591200
- ↑ George Thompson AM, Iancu CV, Neet KE, Dean JV, Choe JY. Differences in salicylic acid glucose conjugations by UGT74F1 and UGT74F2 from Arabidopsis thaliana. Sci Rep. 2017 Apr 20;7:46629. doi: 10.1038/srep46629. PMID:28425481 doi:http://dx.doi.org/10.1038/srep46629
|
