7awa: Difference between revisions

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<StructureSection load='7awa' size='340' side='right'caption='[[7awa]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
<StructureSection load='7awa' size='340' side='right'caption='[[7awa]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7awa]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AWA FirstGlance]. <br>
<table><tr><td colspan='2'>[[7awa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AWA 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=7awa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7awa OCA], [https://pdbe.org/7awa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7awa RCSB], [https://www.ebi.ac.uk/pdbsum/7awa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7awa ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5&#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=7awa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7awa OCA], [https://pdbe.org/7awa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7awa RCSB], [https://www.ebi.ac.uk/pdbsum/7awa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7awa ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/SSAV_SALTY SSAV_SALTY]] Component of Salmonella pathogenicity island 2 (SPI-2) type III secretion system, required for secretion of some type III-secreted effectors including the SpvB toxin.<ref>PMID:18248436</ref> 
[https://www.uniprot.org/uniprot/SSAV_SALTY SSAV_SALTY] Component of Salmonella pathogenicity island 2 (SPI-2) type III secretion system, required for secretion of some type III-secreted effectors including the SpvB toxin.<ref>PMID:18248436</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial type III secretion systems assemble the axial structures of both injectisomes and flagella. Injectisome type III secretion systems subsequently secrete effector proteins through their hollow needle into a host, requiring co-ordination. In the Salmonella enterica serovar Typhimurium SPI-2 injectisome, this switch is triggered by sensing the neutral pH of the host cytoplasm. Central to specificity switching is a nonameric SctV protein with an N-terminal transmembrane domain and a toroidal C-terminal cytoplasmic domain. A 'gatekeeper' complex interacts with the SctV cytoplasmic domain in a pH dependent manner, facilitating translocon secretion while repressing effector secretion through a poorly understood mechanism. To better understand the role of SctV in SPI-2 translocon-effector specificity switching, we purified full-length SctV and determined its toroidal cytoplasmic region's structure using cryo-EM. Structural comparisons and molecular dynamics simulations revealed that the cytoplasmic torus is stabilized by its core subdomain 3, about which subdomains 2 and 4 hinge, varying the flexible outside cleft implicated in gatekeeper and substrate binding. In light of patterns of surface conservation, deprotonation, and structural motion, the location of previously identified critical residues suggest that gatekeeper binds a cleft buried between neighboring subdomain 4s. Simulations suggest that a local pH change from 5 to 7.2 stabilizes the subdomain 3 hinge and narrows the central aperture of the nonameric torus. Our results are consistent with a model of local pH sensing at SctV, where pH-dependent dynamics of SctV cytoplasmic domain affect binding of gatekeeper complex.
 
Structure of the cytoplasmic domain of SctV (SsaV) from the Salmonella SPI-2 injectisome and implications for a pH sensing mechanism.,Matthews-Palmer TRS, Gonzalez-Rodriguez N, Calcraft T, Lagercrantz S, Zachs T, Yu XJ, Grabe GJ, Holden DW, Nans A, Rosenthal PB, Rouse SL, Beeby M J Struct Biol. 2021 Mar 26;213(2):107729. doi: 10.1016/j.jsb.2021.107729. PMID:33774138<ref>PMID:33774138</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7awa" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Beeby, M]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]]
[[Category: Calcraft, T]]
[[Category: Beeby M]]
[[Category: Gonzalez-Rodriguez, N]]
[[Category: Calcraft T]]
[[Category: Grabe, G]]
[[Category: Gonzalez-Rodriguez N]]
[[Category: Holden, D]]
[[Category: Grabe G]]
[[Category: Lagercrantz, S]]
[[Category: Holden D]]
[[Category: Matthews-Palmer, T R.S]]
[[Category: Lagercrantz S]]
[[Category: Nans, A]]
[[Category: Matthews-Palmer TRS]]
[[Category: Rosenthal, P]]
[[Category: Nans A]]
[[Category: Rouse, S]]
[[Category: Rosenthal P]]
[[Category: Yu, X J]]
[[Category: Rouse S]]
[[Category: Zachs, T]]
[[Category: Yu XJ]]
[[Category: Export apparatus]]
[[Category: Zachs T]]
[[Category: Protein transport]]
[[Category: T3ss]]
[[Category: Type iii secretion]]

Latest revision as of 07:46, 1 May 2024

SctV (SsaV) cytoplasmic domain

7awa, resolution 3.50Å

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