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| | <StructureSection load='7m0o' size='340' side='right'caption='[[7m0o]], [[Resolution|resolution]] 1.62Å' scene=''> | | <StructureSection load='7m0o' size='340' side='right'caption='[[7m0o]], [[Resolution|resolution]] 1.62Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7m0o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"streptomyces_sviceus"_dietz_in_hanka_and_dietz_1973 "streptomyces sviceus" dietz in hanka and dietz 1973]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7M0O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7M0O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7m0o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sviceus Streptomyces sviceus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7M0O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7M0O FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.62Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aroA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=285530 "Streptomyces sviceus" Dietz in Hanka and Dietz 1973])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/3-phosphoshikimate_1-carboxyvinyltransferase 3-phosphoshikimate 1-carboxyvinyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.19 2.5.1.19] </span></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=7m0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m0o OCA], [https://pdbe.org/7m0o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m0o RCSB], [https://www.ebi.ac.uk/pdbsum/7m0o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m0o ProSAT]</span></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=7m0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m0o OCA], [https://pdbe.org/7m0o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m0o RCSB], [https://www.ebi.ac.uk/pdbsum/7m0o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m0o ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/B5HND8_9ACTN B5HND8_9ACTN]] Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.[HAMAP-Rule:MF_00210]
| + | [https://www.uniprot.org/uniprot/B5HND8_9ACTN B5HND8_9ACTN] Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.[HAMAP-Rule:MF_00210] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 7m0o" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 7m0o" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[EPSP synthase 3D structures|EPSP synthase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Streptomyces sviceus dietz in hanka and dietz 1973]] | |
| - | [[Category: 3-phosphoshikimate 1-carboxyvinyltransferase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chekan, J R]] | + | [[Category: Streptomyces sviceus]] |
| - | [[Category: Nair, S K]] | + | [[Category: Chekan JR]] |
| - | [[Category: 5-enolpyruvylshikimate-3-phosphate synthase]] | + | [[Category: Nair SK]] |
| - | [[Category: Biosynthetic protein]]
| + | |
| - | [[Category: Epsp]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
B5HND8_9ACTN Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.[HAMAP-Rule:MF_00210]
Publication Abstract from PubMed
Natural and modified versions of the 5-enolpyruvylshikimate-3-phosphate synthase (epsps) gene have been used to confer tolerance to the broad-spectrum herbicide glyphosate in a variety of commercial crops. The most widely utilized trait was obtained from the Agrobacterium tumefaciens strain CP4 and has been commercialized in several glyphosate-tolerant crops. The EPSPS gene products are enzymes that have been divided into three classes based on sequence similarity, sensitivity to glyphosate, and steady-state catalytic parameters. Herein, we describe the informatics-guided identification and biochemical and structural characterization of a novel EPSPS from Streptomyces sviceus (DGT-28 EPSPS). The data suggest DGT-28 EPSPS and other closely related homologues exemplify a distinct new class (Class IV) of EPSPS enzymes that display intrinsic tolerance to high concentrations of glyphosate (Ki >/= 5000 muM). We further demonstrate that dgt-28 epsps, when transformed into stable plants, provides robust (>/=4x field rates) vegetative/reproductive herbicide tolerance and has utility in weed-control systems comparable to that of commercialized events.
Characterization of a Glyphosate-Tolerant Enzyme from Streptomyces svecius: A Distinct Class of 5-Enolpyruvylshikimate-3-phosphate Synthases.,Griffin SL, Chekan JR, Lira JM, Robinson AE, Yerkes CN, Siehl DL, Wright TR, Nair SK, Cicchillo RM J Agric Food Chem. 2021 Apr 7. doi: 10.1021/acs.jafc.1c00439. PMID:33826316[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Griffin SL, Chekan JR, Lira JM, Robinson AE, Yerkes CN, Siehl DL, Wright TR, Nair SK, Cicchillo RM. Characterization of a Glyphosate-Tolerant Enzyme from Streptomyces svecius: A Distinct Class of 5-Enolpyruvylshikimate-3-phosphate Synthases. J Agric Food Chem. 2021 Apr 7. doi: 10.1021/acs.jafc.1c00439. PMID:33826316 doi:http://dx.doi.org/10.1021/acs.jafc.1c00439
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