2gwm: Difference between revisions

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<StructureSection load='2gwm' size='340' side='right'caption='[[2gwm]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='2gwm' size='340' side='right'caption='[[2gwm]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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 [https://proteopedia.org/fgij/fg.htm?mol=2GWM FirstGlance]. <br>
<table><tr><td colspan='2'>[[2gwm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2GWM FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.5&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2gwl|2gwl]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2gwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gwm OCA], [https://pdbe.org/2gwm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gwm RCSB], [https://www.ebi.ac.uk/pdbsum/2gwm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gwm 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=2gwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gwm OCA], [https://pdbe.org/2gwm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gwm RCSB], [https://www.ebi.ac.uk/pdbsum/2gwm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gwm ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://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).  
[https://www.uniprot.org/uniprot/SPVB_SALTM SPVB_SALTM] Mono-ADP-ribosylates eukaryotic muscle and non-muscle actin on 'Arg-177'. ADP-ribosylates all actins tested, has more activity on nonmuscle beta/gamma-actin than on muscle alpha-actin. Prefers monomeric G-actin but can weakly ADP-ribosylate F-actin. 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.<ref>PMID:10972829</ref> <ref>PMID:16430223</ref> <ref>PMID:16905096</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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].
</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;">
== Publication Abstract from PubMed ==
Salmonella 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<ref>PMID:16905096</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2gwm" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Margarit, S M]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: Stebbins, C E]]
[[Category: Margarit SM]]
[[Category: Adp-ribosyltransferase]]
[[Category: Stebbins CE]]
[[Category: Salmonella]]
[[Category: Spvb]]
[[Category: Toxin]]
[[Category: Transferase]]

Latest revision as of 12:30, 14 February 2024

Crystal structure of the Salmonella SpvB ATR DomainCrystal structure of the Salmonella SpvB ATR Domain

Structural highlights

2gwm is a 1 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SPVB_SALTM Mono-ADP-ribosylates eukaryotic muscle and non-muscle actin on 'Arg-177'. ADP-ribosylates all actins tested, has more activity on nonmuscle beta/gamma-actin than on muscle alpha-actin. Prefers monomeric G-actin but can weakly ADP-ribosylate F-actin. 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.[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Otto H, Tezcan-Merdol D, Girisch R, Haag F, Rhen M, Koch-Nolte F. The spvB gene-product of the Salmonella enterica virulence plasmid is a mono(ADP-ribosyl)transferase. Mol Microbiol. 2000 Sep;37(5):1106-15. PMID:10972829 doi:10.1046/j.1365-2958.2000.02064.x
  2. ↑ Hochmann H, Pust S, von Figura G, Aktories K, Barth H. Salmonella enterica SpvB ADP-ribosylates actin at position arginine-177-characterization of the catalytic domain within the SpvB protein and a comparison to binary clostridial actin-ADP-ribosylating toxins. Biochemistry. 2006 Jan 31;45(4):1271-7. PMID:16430223 doi:10.1021/bi051810w
  3. ↑ Margarit SM, Davidson W, Frego L, Stebbins CE. A steric antagonism of actin polymerization by a salmonella virulence protein. Structure. 2006 Aug;14(8):1219-29. PMID:16905096 doi:10.1016/j.str.2006.05.022

2gwm, resolution 1.50Å

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