2gwm: Difference between revisions
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<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=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2gwm]] is a 1 chain structure | <table><tr><td colspan='2'>[[2gwm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GWM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GWM FirstGlance]. <br> | ||
</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://www.rcsb.org/pdb/explore.do?structureId=2gwm RCSB], [http://www.ebi.ac.uk/pdbsum/2gwm PDBsum]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/ | [[http://www.uniprot.org/uniprot/SPVB_SALEN 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2gwm" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Margarit, S M]] | [[Category: Margarit, S M]] | ||
[[Category: Stebbins, C E]] | [[Category: Stebbins, C E]] | ||
Revision as of 17:39, 11 September 2015
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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