2fm8: Difference between revisions

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<StructureSection load='2fm8' size='340' side='right'caption='[[2fm8]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='2fm8' size='340' side='right'caption='[[2fm8]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2fm8]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FM8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FM8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2fm8]] is a 3 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=2FM8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FM8 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=2fm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fm8 OCA], [https://pdbe.org/2fm8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fm8 RCSB], [https://www.ebi.ac.uk/pdbsum/2fm8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fm8 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]] 2.2&#8491;</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=2fm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fm8 OCA], [https://pdbe.org/2fm8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fm8 RCSB], [https://www.ebi.ac.uk/pdbsum/2fm8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fm8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/SPAK_SALTY SPAK_SALTY]] Involved in a secretory pathway responsible for the surface presentation of determinants needed for the entry of Salmonella species into mammalian cells. Chaperone specialized in the storage of effectors within the bacterial cytoplasm, maintaining them in a secretion-competent state, and allowing their immediate delivery to target cells upon contact of the bacterium with the host cells. Has been shown to chaperone SopA, SopE, SopE2 and SipA.<ref>PMID:16547027</ref> <ref>PMID:16507363</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> 
[https://www.uniprot.org/uniprot/SPAK_SALTY SPAK_SALTY] Involved in a secretory pathway responsible for the surface presentation of determinants needed for the entry of Salmonella species into mammalian cells. Chaperone specialized in the storage of effectors within the bacterial cytoplasm, maintaining them in a secretion-competent state, and allowing their immediate delivery to target cells upon contact of the bacterium with the host cells. Has been shown to chaperone SopA, SopE, SopE2 and SipA.<ref>PMID:16547027</ref> <ref>PMID:16507363</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=2fm8 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=2fm8 ConSurf].
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<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2fm8" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lilic, M]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: Stebbins, C E]]
[[Category: Lilic M]]
[[Category: Vujanac, M]]
[[Category: Stebbins CE]]
[[Category: Bacterial]]
[[Category: Vujanac M]]
[[Category: Chaperone]]
[[Category: Chaperone-cell invasion complex]]
[[Category: Protein folding]]
[[Category: Salmonella]]
[[Category: Translocation]]
[[Category: Type iii secretion]]
[[Category: Virulence]]
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