1q5z
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1q5z]] 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=1Q5Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q5Z FirstGlance]. <br> | <table><tr><td colspan='2'>[[1q5z]] 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=1Q5Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q5Z FirstGlance]. <br> | ||
| - | </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=1q5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q5z OCA], [https://pdbe.org/1q5z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q5z RCSB], [https://www.ebi.ac.uk/pdbsum/1q5z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q5z 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]] 1.8Å</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=1q5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q5z OCA], [https://pdbe.org/1q5z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q5z RCSB], [https://www.ebi.ac.uk/pdbsum/1q5z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q5z ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/SIPA_SALTY SIPA_SALTY] Actin-binding protein that interferes with host cell actin cytoskeleton. It stimulates actin polymerization and counteracts F-actin destabilizing proteins. Potentiates SipC activity; both are required for an efficient bacterial internalization. In vitro, forms a complex with host cell protein T-plastin increasing actin bundling. It inhibits ADF/cofilin-directed depolymerization both by preventing binding of ADF and cofilin and by displacing them from F-actin. Also protects F-actin from gelsolin-directed severing and reanneals gelsolin-severed F-actin fragments.<ref>PMID:10092234</ref> <ref>PMID:14992720</ref> | [https://www.uniprot.org/uniprot/SIPA_SALTY SIPA_SALTY] Actin-binding protein that interferes with host cell actin cytoskeleton. It stimulates actin polymerization and counteracts F-actin destabilizing proteins. Potentiates SipC activity; both are required for an efficient bacterial internalization. In vitro, forms a complex with host cell protein T-plastin increasing actin bundling. It inhibits ADF/cofilin-directed depolymerization both by preventing binding of ADF and cofilin and by displacing them from F-actin. Also protects F-actin from gelsolin-directed severing and reanneals gelsolin-severed F-actin fragments.<ref>PMID:10092234</ref> <ref>PMID:14992720</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Like many bacterial pathogens, Salmonella spp. use a type III secretion system to inject virulence proteins into host cells. The Salmonella invasion protein A (SipA) binds host actin, enhances its polymerization near adherent extracellular bacteria, and contributes to cytoskeletal rearrangements that internalize the pathogen. By combining x-ray crystallography of SipA with electron microscopy and image analysis of SipA-actin filaments, we show that SipA functions as a "molecular staple," in which a globular domain and two nonglobular "arms" mechanically stabilize the filament by tethering actin subunits in opposing strands. Deletion analysis of the tethering arms provides strong support for this model. | ||
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| - | Salmonella SipA polymerizes actin by stapling filaments with nonglobular protein arms.,Lilic M, Galkin VE, Orlova A, VanLoock MS, Egelman EH, Stebbins CE Science. 2003 Sep 26;301(5641):1918-21. PMID:14512630<ref>PMID:14512630</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1q5z" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal Structure of the C-terminal Actin Binding Domain of Salmonella Invasion Protein A (SipA)
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