2fm9

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<StructureSection load='2fm9' size='340' side='right'caption='[[2fm9]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='2fm9' size='340' side='right'caption='[[2fm9]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2fm9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FM9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FM9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2fm9]] 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=2FM9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FM9 FirstGlance]. <br>
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</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=2fm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fm9 OCA], [https://pdbe.org/2fm9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fm9 RCSB], [https://www.ebi.ac.uk/pdbsum/2fm9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fm9 ProSAT]</span></td></tr>
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</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&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fm9 OCA], [https://pdbe.org/2fm9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fm9 RCSB], [https://www.ebi.ac.uk/pdbsum/2fm9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fm9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Salmonella invasion protein A (SipA) is translocated into host cells by a type III secretion system (T3SS) and comprises two regions: one domain binds its cognate type III secretion chaperone, InvB, in the bacterium to facilitate translocation, while a second domain functions in the host cell, contributing to bacterial uptake by polymerizing actin. We present here the crystal structures of the SipA chaperone binding domain (CBD) alone and in complex with InvB. The SipA CBD is found to consist of a nonglobular polypeptide as well as a large globular domain, both of which are necessary for binding to InvB. We also identify a structural motif that may direct virulence factors to their cognate chaperones in a diverse range of pathogenic bacteria. Disruption of this structural motif leads to a destabilization of several chaperone-substrate complexes from different species, as well as an impairment of secretion in Salmonella.
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A common structural motif in the binding of virulence factors to bacterial secretion chaperones.,Lilic M, Vujanac M, Stebbins CE Mol Cell. 2006 Mar 3;21(5):653-64. PMID:16507363<ref>PMID:16507363</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2fm9" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lilic, M]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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[[Category: Stebbins, C E]]
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[[Category: Lilic M]]
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[[Category: Vujanac, M]]
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[[Category: Stebbins CE]]
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[[Category: Bacterial]]
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[[Category: Vujanac M]]
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[[Category: Cell invasion]]
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[[Category: Salmonella]]
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[[Category: Sipa]]
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[[Category: Type ii secretion]]
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[[Category: Virulence]]
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Current revision

Structure of Salmonella SipA residues 48-264

PDB ID 2fm9

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