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| | <StructureSection load='1oxw' size='340' side='right'caption='[[1oxw]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='1oxw' size='340' side='right'caption='[[1oxw]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1oxw]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Heartleaf_nightshade Heartleaf nightshade]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OXW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OXW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1oxw]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Solanum_cardiophyllum Solanum cardiophyllum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OXW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OXW FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2.2Å</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=1oxw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oxw OCA], [http://pdbe.org/1oxw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oxw RCSB], [http://www.ebi.ac.uk/pdbsum/1oxw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1oxw ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1oxw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oxw OCA], [https://pdbe.org/1oxw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oxw RCSB], [https://www.ebi.ac.uk/pdbsum/1oxw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oxw ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PAT17_SOLCD PAT17_SOLCD] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ox/1oxw_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ox/1oxw_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Heartleaf nightshade]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Alibhai, M F]] | + | [[Category: Solanum cardiophyllum]] |
| - | [[Category: Brown, S M]] | + | [[Category: Alibhai MF]] |
| - | [[Category: Krieger, E]] | + | [[Category: Brown SM]] |
| - | [[Category: Moshiri, F]] | + | [[Category: Krieger E]] |
| - | [[Category: Pershing, J C]] | + | [[Category: Moshiri F]] |
| - | [[Category: Purcell, J P]] | + | [[Category: Pershing JC]] |
| - | [[Category: Rydel, T J]] | + | [[Category: Purcell JP]] |
| - | [[Category: Stallings, W C]] | + | [[Category: Rydel TJ]] |
| - | [[Category: Williams, J M]] | + | [[Category: Stallings WC]] |
| - | [[Category: Alpha/beta class fold with approximately three layer]]
| + | [[Category: Williams JM]] |
| - | [[Category: Alpha/beta/alpha in content. possesses a central six-stranded beta sheet with alpha-helices front & back]]
| + | |
| - | [[Category: Plant protein]]
| + | |
| Structural highlights
Function
PAT17_SOLCD
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Patatin is a nonspecific lipid acyl hydrolase that accounts for approximately 40% of the total soluble protein in mature potato tubers, and it has potent insecticidal activity against the corn rootworm. We determined the X-ray crystal structure of a His-tagged variant of an isozyme of patatin, Pat17, to 2.2 A resolution, employing SeMet multiwavelength anomalous dispersion (MAD) phasing methods. The patatin crystal structure has three molecules in the asymmetric unit, an R-factor of 22.0%, and an R(free) of 27.2% (for 10% of the data not included in the refinement) and includes 498 water molecules. The structure notably revealed that patatin has a Ser-Asp catalytic dyad and an active site like that of human cytosolic phospholipase A(2) (cPLA(2)) [Dessen, A., et al. (1999) Cell 97, 349-360]. In addition, patatin has a folding topology related to that of the catalytic domain of cPLA(2) and unlike the canonical alpha/beta-hydrolase fold. The structure confirms our site-directed mutagenesis and bioactivity data that initially suggested patatin possessed a Ser-Asp catalytic dyad. Alanine-scanning mutagenesis revealed that Ser77 and Asp215 were critical for both esterase and bioactivity, consistent with prior work implicating a Ser residue [Strickland, J. H., et al. (1995) Plant Physiol. 109, 667-674] and a Ser-Asp dyad [Hirschberg, H. J. H. B., et al. (2001) Eur. J. Biochem. 268, 5037-5044] in patatin's catalytic activity. The crystal structure aids the understanding of other structure-function relationships in patatin. Patatin does not display interfacial activation, a hallmark feature of lipases, and this is likely due to the fact that it lacks a flexible lid that can shield the active site.
The crystal structure, mutagenesis, and activity studies reveal that patatin is a lipid acyl hydrolase with a Ser-Asp catalytic dyad.,Rydel TJ, Williams JM, Krieger E, Moshiri F, Stallings WC, Brown SM, Pershing JC, Purcell JP, Alibhai MF Biochemistry. 2003 Jun 10;42(22):6696-708. PMID:12779324[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rydel TJ, Williams JM, Krieger E, Moshiri F, Stallings WC, Brown SM, Pershing JC, Purcell JP, Alibhai MF. The crystal structure, mutagenesis, and activity studies reveal that patatin is a lipid acyl hydrolase with a Ser-Asp catalytic dyad. Biochemistry. 2003 Jun 10;42(22):6696-708. PMID:12779324 doi:10.1021/bi027156r
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