2gwm: Difference between revisions
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==Crystal structure of the Salmonella SpvB ATR Domain== | ==Crystal structure of the Salmonella SpvB ATR Domain== | ||
<StructureSection load='2gwm' size='340' side='right' caption='[[2gwm]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='2gwm' size='340' side='right' caption='[[2gwm]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gwl|2gwl]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gwl|2gwl]]</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=2gwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gwm OCA], [http://pdbe.org/2gwm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gwm RCSB], [http://www.ebi.ac.uk/pdbsum/2gwm PDBsum]</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=2gwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gwm OCA], [http://pdbe.org/2gwm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gwm RCSB], [http://www.ebi.ac.uk/pdbsum/2gwm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2gwm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2gwm ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 11:02, 18 October 2017
Crystal structure of the Salmonella SpvB ATR DomainCrystal structure of the Salmonella SpvB ATR Domain
Structural highlights
Function[SPVB_SALEN] Mono-ADP-ribosylates eukaryotic muscle and non-muscle actin on 'Arg-177'. ADP-ribosylation prevents the polymerization of G-actin to F-actin, causing actin filament depolymerization, destruction of the cytoskeleton and cytotoxicity. Does not possess NAD(+)-glycohydrolase activity, unlike most mART enzymes (By similarity). 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 PubMedSalmonella spp. require the ADP-ribosyltransferase activity of the SpvB protein for intracellular growth and systemic virulence. SpvB covalently modifies actin, causing cytoskeletal disruption and apoptosis. We report here the crystal structure of the catalytic domain of SpvB, and we show by mass spectrometric analysis that SpvB modifies actin at Arg177, inhibiting its ATPase activity. We also describe two crystal structures of SpvB-modified, polymerization-deficient actin. These structures reveal that ADP-ribosylation does not lead to dramatic conformational changes in actin, suggesting a model in which this large family of toxins inhibits actin polymerization primarily through steric disruption of intrafilament contacts. A steric antagonism of actin polymerization by a salmonella virulence protein.,Margarit SM, Davidson W, Frego L, Stebbins CE Structure. 2006 Aug;14(8):1219-29. PMID:16905096[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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