3tul: Difference between revisions
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==Crystal structure of N-terminal region of Type III Secretion Major Translocator SipB (residues 82-226)== | ==Crystal structure of N-terminal region of Type III Secretion Major Translocator SipB (residues 82-226)== | ||
<StructureSection load='3tul' size='340' side='right' caption='[[3tul]], [[Resolution|resolution]] 2.79Å' scene=''> | <StructureSection load='3tul' size='340' side='right'caption='[[3tul]], [[Resolution|resolution]] 2.79Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3tul]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3tul]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TUL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TUL FirstGlance]. <br> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3u0c|3u0c]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3u0c|3u0c]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sipB, sspB, STM2885 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sipB, sspB, STM2885 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tul OCA], [https://pdbe.org/3tul PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tul RCSB], [https://www.ebi.ac.uk/pdbsum/3tul PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tul ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/SIPB_SALTY SIPB_SALTY]] Required for entry into the host cell through presentation or delivery of SipC at the host cell plasma membrane. Along with SipC, is necessary for the transfer of other effector proteins into the host cell. Induces macrophage apoptosis either by binding and activating the proapoptotic enzyme caspase-1 (caspase-1 dependent), resulting in the release of interleukin-1 beta active form, or by disrupting mitochondria and inducing autophagy (caspase-1 independent). The former is dependent of its membrane-fusion activity. The SipBC complex, in association with its chaperone SicA, is regulated by binding of InvE.<ref>PMID:10051653</ref> <ref>PMID:14662750</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bacillus typhimurium loeffler 1892]] | [[Category: Bacillus typhimurium loeffler 1892]] | ||
[[Category: Large Structures]] | |||
[[Category: Barta, M L]] | [[Category: Barta, M L]] | ||
[[Category: Dickenson, N E]] | [[Category: Dickenson, N E]] | ||