6f2d
From Proteopedia
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<StructureSection load='6f2d' size='340' side='right' caption='[[6f2d]], [[Resolution|resolution]] 4.20Å' scene=''> | <StructureSection load='6f2d' size='340' side='right' caption='[[6f2d]], [[Resolution|resolution]] 4.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6f2d]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F2D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6f2d]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_cholerae-suis"_smith_1894 "bacillus cholerae-suis" smith 1894]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F2D FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6f2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f2d OCA], [http://pdbe.org/6f2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f2d RCSB], [http://www.ebi.ac.uk/pdbsum/6f2d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f2d ProSAT]</span></td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fliP, LTSERUB_0568 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28901 "Bacillus cholerae-suis" Smith 1894]), fliR, flaP, STM1981 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28901 "Bacillus cholerae-suis" Smith 1894]), fliQ, flaQ, STY2188, t0897 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28901 "Bacillus cholerae-suis" Smith 1894])</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6f2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f2d OCA], [http://pdbe.org/6f2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f2d RCSB], [http://www.ebi.ac.uk/pdbsum/6f2d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f2d ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/G5QE81_SALRU G5QE81_SALRU]] Plays a role in the flagellum-specific transport system.[RuleBase:RU362069] [[http://www.uniprot.org/uniprot/FLIQ_SALTI FLIQ_SALTI]] Required for the assembly of the rivet at the earliest stage of flagellar biosynthesis. [[http://www.uniprot.org/uniprot/FLIR_SALTY FLIR_SALTY]] Role in flagellar biosynthesis. | [[http://www.uniprot.org/uniprot/G5QE81_SALRU G5QE81_SALRU]] Plays a role in the flagellum-specific transport system.[RuleBase:RU362069] [[http://www.uniprot.org/uniprot/FLIQ_SALTI FLIQ_SALTI]] Required for the assembly of the rivet at the earliest stage of flagellar biosynthesis. [[http://www.uniprot.org/uniprot/FLIR_SALTY FLIR_SALTY]] Role in flagellar biosynthesis. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Export of proteins through type III secretion systems is critical for motility and virulence of many major bacterial pathogens. Three putative integral membrane proteins (FliP, FliQ, FliR) are suggested to form the core of an export gate in the inner membrane, but their structure, assembly and location within the final nanomachine remain unclear. Here, we present the cryoelectron microscopy structure of the Salmonella Typhimurium FliP-FliQ-FliR complex at 4.2 A. None of the subunits adopt canonical integral membrane protein topologies, and common helix-turn-helix structural elements allow them to form a helical assembly with 5:4:1 stoichiometry. Fitting of the structure into reconstructions of intact secretion systems, combined with cross-linking, localize the export gate as a core component of the periplasmic portion of the machinery. This study thereby identifies the export gate as a key element of the secretion channel and implies that it primes the helical architecture of the components assembling downstream. | ||
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| + | Structure of the core of the type III secretion system export apparatus.,Kuhlen L, Abrusci P, Johnson S, Gault J, Deme J, Caesar J, Dietsche T, Mebrhatu MT, Ganief T, Macek B, Wagner S, Robinson CV, Lea SM Nat Struct Mol Biol. 2018 Jul;25(7):583-590. doi: 10.1038/s41594-018-0086-9. Epub, 2018 Jul 2. PMID:29967543<ref>PMID:29967543</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6f2d" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bacillus cholerae-suis smith 1894]] | ||
[[Category: Abrusci, P]] | [[Category: Abrusci, P]] | ||
[[Category: Johnson, S]] | [[Category: Johnson, S]] | ||
Revision as of 09:49, 18 July 2018
A FliPQR complex forms the core of the Salmonella type III secretion system export apparatus.
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