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| | <StructureSection load='6e1q' size='340' side='right'caption='[[6e1q]], [[Resolution|resolution]] 2.15Å' scene=''> | | <StructureSection load='6e1q' size='340' side='right'caption='[[6e1q]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6e1q]] is a 1 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=6E1Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E1Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6e1q]] is a 1 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=6E1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E1Q FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CFA:(2,4-DICHLOROPHENOXY)ACETIC+ACID'>CFA</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]] 2.148Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At5g13370, At5g13370/T22N19_20, T22N19.20, T22N19_20 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CFA:(2,4-DICHLOROPHENOXY)ACETIC+ACID'>CFA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=6e1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e1q OCA], [http://pdbe.org/6e1q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e1q RCSB], [http://www.ebi.ac.uk/pdbsum/6e1q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e1q 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=6e1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e1q OCA], [https://pdbe.org/6e1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e1q RCSB], [https://www.ebi.ac.uk/pdbsum/6e1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e1q ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/GH315_ARATH GH315_ARATH] Indole-3-acetic acid-amido (IAA) synthetase that catalyzes the conjugation of amino acids to auxin specifically using the auxin precursor indole-3-butyric acid (IBA) and glutamine and, possibly, cysteine as substrates (PubMed:29462792, PubMed:30315112). Displays high catalytic activity with the auxinic phenoxyalkanoic acid herbicides 4-(2,4-dichlorophenoxy)butyric acid (2,4-DB) and to some extent 2,4-dichlorophenoxylacetic acid (2,4-D) as substrates, thus confering resistance to herbicides (PubMed:30315112).<ref>PMID:29462792</ref> <ref>PMID:30315112</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jez, J M]] | + | [[Category: Jez JM]] |
| - | [[Category: Lee, S G]] | + | [[Category: Lee SG]] |
| - | [[Category: Sharp, A M]] | + | [[Category: Sharp AM]] |
| - | [[Category: Acyl acid-amido synthetase]]
| + | |
| - | [[Category: Adenylating enzyme]]
| + | |
| - | [[Category: Adenylation]]
| + | |
| - | [[Category: Hormone modification]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Plant protein]]
| + | |
| Structural highlights
Function
GH315_ARATH Indole-3-acetic acid-amido (IAA) synthetase that catalyzes the conjugation of amino acids to auxin specifically using the auxin precursor indole-3-butyric acid (IBA) and glutamine and, possibly, cysteine as substrates (PubMed:29462792, PubMed:30315112). Displays high catalytic activity with the auxinic phenoxyalkanoic acid herbicides 4-(2,4-dichlorophenoxy)butyric acid (2,4-DB) and to some extent 2,4-dichlorophenoxylacetic acid (2,4-D) as substrates, thus confering resistance to herbicides (PubMed:30315112).[1] [2]
Publication Abstract from PubMed
Herbicide-resistance traits are the most widely used agriculture biotechnology products. Yet, to maintain their effectiveness and to mitigate selection of herbicide-resistant weeds, the discovery of new resistance traits that use different chemical modes of action is essential. In plants, the Gretchen Hagen 3 (GH3) acyl acid amido synthetases catalyze the conjugation of amino acids to jasmonate and auxin phytohormones. This reaction chemistry has not been explored as a possible approach for herbicide modification and inactivation. Here, we examined a set of Arabidopsis GH3 proteins that use the auxins indole-3-acetic acid (IAA) and indole-3-butyric acid (IBA) as substrates along with the corresponding auxinic phenoxyalkanoic acid herbicides 2,4-dichlorophenoxylacetic acid (2,4-D) and 4-(2,4-dichlorophenoxy)butyric acid (2,4-DB). The IBA-specific AtGH3.15 protein displayed high catalytic activity with 2,4-DB, which was comparable to its activity with IBA. Screening of phenoxyalkanoic and phenylalkyl acids indicated that side-chain length of alkanoic and alkyl acids is a key feature of AtGH3.15's substrate preference. The X-ray crystal structure of the AtGH3.15*2,4-DB complex revealed how the herbicide binds in the active site. In root elongation assays, Arabidopsis AtGH3.15-knockout and -overexpression lines grown in the presence of 2,4-DB exhibited hypersensitivity and tolerance, respectively, indicating that the AtGH3.15-catalyzed modification inactivates 2,4-DB. These findings suggest a potential use for AtGH3.15, and perhaps other GH3 proteins, as herbicide-modifying enzymes that employ a mode of action different from those of currently available herbicide resistance traits.
Modification of auxinic phenoxyalkanoic acid herbicides by the acyl acid amido synthetase GH3.15 from Arabidopsis.,Sherp AM, Lee SG, Schraft E, Jez JM J Biol Chem. 2018 Oct 12. pii: RA118.004975. doi: 10.1074/jbc.RA118.004975. PMID:30315112[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sherp AM, Westfall CS, Alvarez S, Jez JM. Arabidopsis thaliana GH3.15 acyl acid amido synthetase has a highly specific substrate preference for the auxin precursor indole-3-butyric acid. J Biol Chem. 2018 Mar 23;293(12):4277-4288. doi: 10.1074/jbc.RA118.002006. Epub, 2018 Feb 8. PMID:29462792 doi:http://dx.doi.org/10.1074/jbc.RA118.002006
- ↑ Sherp AM, Lee SG, Schraft E, Jez JM. Modification of auxinic phenoxyalkanoic acid herbicides by the acyl acid amido synthetase GH3.15 from Arabidopsis. J Biol Chem. 2018 Oct 12. pii: RA118.004975. doi: 10.1074/jbc.RA118.004975. PMID:30315112 doi:http://dx.doi.org/10.1074/jbc.RA118.004975
- ↑ Sherp AM, Lee SG, Schraft E, Jez JM. Modification of auxinic phenoxyalkanoic acid herbicides by the acyl acid amido synthetase GH3.15 from Arabidopsis. J Biol Chem. 2018 Oct 12. pii: RA118.004975. doi: 10.1074/jbc.RA118.004975. PMID:30315112 doi:http://dx.doi.org/10.1074/jbc.RA118.004975
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