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| <SX load='3j1v' size='340' side='right' viewer='molstar' caption='[[3j1v]], [[Resolution|resolution]] 11.70Å' scene=''> | | <SX load='3j1v' size='340' side='right' viewer='molstar' caption='[[3j1v]], [[Resolution|resolution]] 11.70Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3j1v]] is a 15 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=3J1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J1V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3j1v]] is a 15 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=3J1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J1V FirstGlance]. <br> |
- | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4g08|4g08]], [[4g1i|4g1i]], [[3j1w|3j1w]], [[3j1x|3j1x]]</div></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]] 11.7Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">invG, STM2898 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=3j1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j1v OCA], [https://pdbe.org/3j1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j1v RCSB], [https://www.ebi.ac.uk/pdbsum/3j1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j1v ProSAT]</span></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=3j1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j1v OCA], [https://pdbe.org/3j1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j1v RCSB], [https://www.ebi.ac.uk/pdbsum/3j1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j1v ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[https://www.uniprot.org/uniprot/INVG_SALTY INVG_SALTY]] Involved in the invasion of the cells of the intestinal epithelium. Could be necessary for the export of invasion related determinants.
| + | [https://www.uniprot.org/uniprot/SCTC1_SALTY SCTC1_SALTY] Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:9786184, PubMed:27974800, PubMed:30242280). Forms a ring-shaped multimeric structure with an apparent central pore in the outer membrane (PubMed:9786184, PubMed:21385715, PubMed:27974800, PubMed:30242280).<ref>PMID:21385715</ref> <ref>PMID:27974800</ref> <ref>PMID:30242280</ref> <ref>PMID:9786184</ref> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
- | Type III secretion systems (T3SSs) are essential virulence factors used by many Gram-negative bacteria to inject proteins that make eukaryotic host cells accessible to invasion. The T3SS core structure, the needle complex (NC), is a ~3.5 megadalton-sized, oligomeric, membrane-embedded complex. Analyzing cryo-electron microscopy images of top views of NCs or NC substructures from Salmonella typhimurium revealed a 24-fold symmetry for the inner rings and a 15-fold symmetry for the outer rings, giving an overall C3 symmetry. Local refinement and averaging showed the organization of the central core and allowed us to reconstruct a subnanometer composite structure of the NC, which together with confident docking of atomic structures reveal insights into its overall organization and structural requirements during assembly.
| + | The T3SS injectisome is a syringe-shaped macromolecular assembly found in pathogenic Gram-negative bacteria that allows for the direct delivery of virulence effectors into host cells. It is composed of a "basal body", a lock-nut structure spanning both bacterial membranes, and a "needle" that protrudes away from the bacterial surface. A hollow channel spans throughout the apparatus, permitting the translocation of effector proteins from the bacterial cytosol to the host plasma membrane. The basal body is composed largely of three membrane-embedded proteins that form oligomerized concentric rings. Here, we report the crystal structures of three domains of the prototypical Salmonella SPI-1 basal body, and use a new approach incorporating symmetric flexible backbone docking and EM data to produce a model for their oligomeric assembly. The obtained models, validated by biochemical and in vivo assays, reveal the molecular details of the interactions driving basal body assembly, and notably demonstrate a conserved oligomerization mechanism. |
| | | |
- | Three-dimensional model of Salmonella's needle complex at subnanometer resolution.,Schraidt O, Marlovits TC Science. 2011 Mar 4;331(6021):1192-5. PMID:21385715<ref>PMID:21385715</ref>
| + | A Refined Model of the Prototypical Salmonella SPI-1 T3SS Basal Body Reveals the Molecular Basis for Its Assembly.,Bergeron JR, Worrall LJ, Sgourakis NG, Dimaio F, Pfuetzner RA, Felise HB, Vuckovic M, Yu AC, Miller SI, Baker D, Strynadka NC PLoS Pathog. 2013 Apr;9(4):e1003307. doi: 10.1371/journal.ppat.1003307. Epub 2013, Apr 25. PMID:23633951<ref>PMID:23633951</ref> |
| | | |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
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| __TOC__ | | __TOC__ |
| </SX> | | </SX> |
- | [[Category: Bacillus typhimurium loeffler 1892]] | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Baker, D]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium]] |
- | [[Category: Bergeron, J R.C]]
| + | [[Category: Baker D]] |
- | [[Category: Sgourakis, N G]] | + | [[Category: Bergeron JRC]] |
- | [[Category: Strynadka, N J.C]] | + | [[Category: Sgourakis NG]] |
- | [[Category: Cell invasion]] | + | [[Category: Strynadka NJC]] |
- | [[Category: Secretin]] | + | |
- | [[Category: T3ss]]
| + | |
| Structural highlights
Function
SCTC1_SALTY Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:9786184, PubMed:27974800, PubMed:30242280). Forms a ring-shaped multimeric structure with an apparent central pore in the outer membrane (PubMed:9786184, PubMed:21385715, PubMed:27974800, PubMed:30242280).[1] [2] [3] [4]
Publication Abstract from PubMed
The T3SS injectisome is a syringe-shaped macromolecular assembly found in pathogenic Gram-negative bacteria that allows for the direct delivery of virulence effectors into host cells. It is composed of a "basal body", a lock-nut structure spanning both bacterial membranes, and a "needle" that protrudes away from the bacterial surface. A hollow channel spans throughout the apparatus, permitting the translocation of effector proteins from the bacterial cytosol to the host plasma membrane. The basal body is composed largely of three membrane-embedded proteins that form oligomerized concentric rings. Here, we report the crystal structures of three domains of the prototypical Salmonella SPI-1 basal body, and use a new approach incorporating symmetric flexible backbone docking and EM data to produce a model for their oligomeric assembly. The obtained models, validated by biochemical and in vivo assays, reveal the molecular details of the interactions driving basal body assembly, and notably demonstrate a conserved oligomerization mechanism.
A Refined Model of the Prototypical Salmonella SPI-1 T3SS Basal Body Reveals the Molecular Basis for Its Assembly.,Bergeron JR, Worrall LJ, Sgourakis NG, Dimaio F, Pfuetzner RA, Felise HB, Vuckovic M, Yu AC, Miller SI, Baker D, Strynadka NC PLoS Pathog. 2013 Apr;9(4):e1003307. doi: 10.1371/journal.ppat.1003307. Epub 2013, Apr 25. PMID:23633951[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schraidt O, Marlovits TC. Three-dimensional model of Salmonella's needle complex at subnanometer resolution. Science. 2011 Mar 4;331(6021):1192-5. PMID:21385715 doi:10.1126/science.1199358
- ↑ Worrall LJ, Hong C, Vuckovic M, Deng W, Bergeron JR, Majewski DD, Huang RK, Spreter T, Finlay BB, Yu Z, Strynadka NC. Near-atomic-resolution cryo-EM analysis of the Salmonella T3S injectisome basal body. Nature. 2016 Dec 14. doi: 10.1038/nature20576. PMID:27974800 doi:http://dx.doi.org/10.1038/nature20576
- ↑ Hu J, Worrall LJ, Hong C, Vuckovic M, Atkinson CE, Caveney N, Yu Z, Strynadka NCJ. Cryo-EM analysis of the T3S injectisome reveals the structure of the needle and open secretin. Nat Commun. 2018 Sep 21;9(1):3840. doi: 10.1038/s41467-018-06298-8. PMID:30242280 doi:http://dx.doi.org/10.1038/s41467-018-06298-8
- ↑ Crago AM, Koronakis V. Salmonella InvG forms a ring-like multimer that requires the InvH lipoprotein for outer membrane localization. Mol Microbiol. 1998 Oct;30(1):47-56. doi: 10.1046/j.1365-2958.1998.01036.x. PMID:9786184 doi:http://dx.doi.org/10.1046/j.1365-2958.1998.01036.x
- ↑ Bergeron JR, Worrall LJ, Sgourakis NG, Dimaio F, Pfuetzner RA, Felise HB, Vuckovic M, Yu AC, Miller SI, Baker D, Strynadka NC. A Refined Model of the Prototypical Salmonella SPI-1 T3SS Basal Body Reveals the Molecular Basis for Its Assembly. PLoS Pathog. 2013 Apr;9(4):e1003307. doi: 10.1371/journal.ppat.1003307. Epub 2013, Apr 25. PMID:23633951 doi:10.1371/journal.ppat.1003307
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