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| | ==Crystal structure of Arabidopsis thaliana SOBER1== | | ==Crystal structure of Arabidopsis thaliana SOBER1== |
| - | <StructureSection load='6avv' size='340' side='right' caption='[[6avv]], [[Resolution|resolution]] 1.51Å' scene=''> | + | <StructureSection load='6avv' size='340' side='right'caption='[[6avv]], [[Resolution|resolution]] 1.51Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6avv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AVV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AVV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6avv]] 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=6AVV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AVV FirstGlance]. <br> |
| - | </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=6avv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6avv OCA], [http://pdbe.org/6avv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6avv RCSB], [http://www.ebi.ac.uk/pdbsum/6avv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6avv ProSAT]</span></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]] 1.5100306Å</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=6avv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6avv OCA], [https://pdbe.org/6avv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6avv RCSB], [https://www.ebi.ac.uk/pdbsum/6avv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6avv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SOBR1_ARATH SOBR1_ARATH]] Possesses carboxylesterase activity in vitro with a preference for short acyl chain substrates. Functions as a negative regulator of the hypersensitive response (HR) triggered by the bacterial type III effector protein AvrBsT (PubMed:17293566). Possesses phospholipase A2 (PLA2) activity and hydrolyzes phosphatidylcholine (PC), a lipid that is hydrolyzed by phospholipase D (PLD) to produce phosphatidic acid (PA). Required to suppress AvrBsT-dependent HR and PLD-dependent production of PA in response to AvrBsT elicitation (PubMed:19918071).<ref>PMID:17293566</ref> <ref>PMID:19918071</ref> | + | [https://www.uniprot.org/uniprot/SOBR1_ARATH SOBR1_ARATH] Possesses carboxylesterase activity in vitro with a preference for short acyl chain substrates. Functions as a negative regulator of the hypersensitive response (HR) triggered by the bacterial type III effector protein AvrBsT (PubMed:17293566). Possesses phospholipase A2 (PLA2) activity and hydrolyzes phosphatidylcholine (PC), a lipid that is hydrolyzed by phospholipase D (PLD) to produce phosphatidic acid (PA). Required to suppress AvrBsT-dependent HR and PLD-dependent production of PA in response to AvrBsT elicitation (PubMed:19918071).<ref>PMID:17293566</ref> <ref>PMID:19918071</ref> |
| | <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 6avv" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6avv" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Carboxylesterase 3D structures|Carboxylesterase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Burger, M]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Chory, J]] | + | [[Category: Large Structures]] |
| - | [[Category: Willige, B C]] | + | [[Category: Burger M]] |
| - | [[Category: Alpha/beta hydrolase]] | + | [[Category: Chory J]] |
| - | [[Category: Hydrolase]] | + | [[Category: Willige BC]] |
| - | [[Category: Hypersensitive response]]
| + | |
| - | [[Category: Plant deacetylase]]
| + | |
| Structural highlights
Function
SOBR1_ARATH Possesses carboxylesterase activity in vitro with a preference for short acyl chain substrates. Functions as a negative regulator of the hypersensitive response (HR) triggered by the bacterial type III effector protein AvrBsT (PubMed:17293566). Possesses phospholipase A2 (PLA2) activity and hydrolyzes phosphatidylcholine (PC), a lipid that is hydrolyzed by phospholipase D (PLD) to produce phosphatidic acid (PA). Required to suppress AvrBsT-dependent HR and PLD-dependent production of PA in response to AvrBsT elicitation (PubMed:19918071).[1] [2]
Publication Abstract from PubMed
Several Pseudomonas and Xanthomonas species are plant pathogens that infect the model organism Arabidopsis thaliana and important crops such as Brassica. Resistant plants contain the infection by rapid cell death of the infected area through the hypersensitive response (HR). A family of highly related alpha/beta hydrolases is involved in diverse processes in all domains of life. Functional details of their catalytic machinery, however, remained unclear. We report the crystal structures of alpha/beta hydrolases representing two different clades of the family, including the protein SOBER1, which suppresses AvrBsT-incited HR in Arabidopsis. Our results reveal a unique hydrophobic anchor mechanism that defines a previously unknown family of protein deacetylases. Furthermore, this study identifies a lid-loop as general feature for substrate turnover in acyl-protein thioesterases and the described family of deacetylases. Furthermore, we found that SOBER1's biological function is not restricted to Arabidopsis thaliana and not limited to suppress HR induced by AvrBsT.
A hydrophobic anchor mechanism defines a deacetylase family that suppresses host response against YopJ effectors.,Burger M, Willige BC, Chory J Nat Commun. 2017 Dec 19;8(1):2201. doi: 10.1038/s41467-017-02347-w. PMID:29259199[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cunnac S, Wilson A, Nuwer J, Kirik A, Baranage G, Mudgett MB. A conserved carboxylesterase is a SUPPRESSOR OF AVRBST-ELICITED RESISTANCE in Arabidopsis. Plant Cell. 2007 Feb;19(2):688-705. Epub 2007 Feb 9. PMID:17293566 doi:http://dx.doi.org/tpc.106.048710
- ↑ Kirik A, Mudgett MB. SOBER1 phospholipase activity suppresses phosphatidic acid accumulation and plant immunity in response to bacterial effector AvrBsT. Proc Natl Acad Sci U S A. 2009 Dec 1;106(48):20532-7. doi:, 10.1073/pnas.0903859106. Epub 2009 Nov 16. PMID:19918071 doi:http://dx.doi.org/10.1073/pnas.0903859106
- ↑ Burger M, Willige BC, Chory J. A hydrophobic anchor mechanism defines a deacetylase family that suppresses host response against YopJ effectors. Nat Commun. 2017 Dec 19;8(1):2201. doi: 10.1038/s41467-017-02347-w. PMID:29259199 doi:http://dx.doi.org/10.1038/s41467-017-02347-w
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