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| | ==Atomic model of the Type-III Secretion System Needle== | | ==Atomic model of the Type-III Secretion System Needle== |
| - | <StructureSection load='2lpz' size='340' side='right' caption='[[2lpz]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='2lpz' size='340' side='right'caption='[[2lpz]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2lpz]] is a 29 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar typhimurium]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LPZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LPZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2lpz]] is a 29 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LPZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LPZ FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">prgI, STM2873 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 Salmonella enterica subsp. enterica serovar Typhimurium])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solid-state NMR</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=2lpz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lpz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lpz RCSB], [http://www.ebi.ac.uk/pdbsum/2lpz PDBsum]</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=2lpz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lpz OCA], [https://pdbe.org/2lpz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lpz RCSB], [https://www.ebi.ac.uk/pdbsum/2lpz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lpz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PRGI_SALTY PRGI_SALTY]] Required for invasion of epithelial cells. | + | [https://www.uniprot.org/uniprot/PRGI_SALTY PRGI_SALTY] Required for invasion of epithelial cells. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | 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> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 2lpz" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Salmonella enterica subsp. enterica serovar typhimurium]] | + | [[Category: Large Structures]] |
| - | [[Category: Baker, D]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium]] |
| - | [[Category: Becker, S]] | + | [[Category: Baker D]] |
| - | [[Category: Giller, K]] | + | [[Category: Becker S]] |
| - | [[Category: Goosmann, C]] | + | [[Category: Giller K]] |
| - | [[Category: Griesinger, C]] | + | [[Category: Goosmann C]] |
| - | [[Category: Gupta, R]] | + | [[Category: Griesinger C]] |
| - | [[Category: Kolbe, M G]] | + | [[Category: Gupta R]] |
| - | [[Category: Lange, A]] | + | [[Category: Kolbe MG]] |
| - | [[Category: Loquet, A]] | + | [[Category: Lange A]] |
| - | [[Category: Riedel, D]] | + | [[Category: Loquet A]] |
| - | [[Category: Sgourakis, N G]] | + | [[Category: Riedel D]] |
| - | [[Category: Filament]]
| + | [[Category: Sgourakis NG]] |
| - | [[Category: Helical assembly]]
| + | |
| - | [[Category: Needle]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| - | [[Category: Type three secretion system]]
| + | |
| Structural highlights
Function
PRGI_SALTY Required for invasion of epithelial cells.
Publication Abstract from PubMed
Pathogenic bacteria using a type III secretion system (T3SS) to manipulate host cells cause many different infections including Shigella dysentery, typhoid fever, enterohaemorrhagic colitis and bubonic plague. An essential part of the T3SS is a hollow needle-like protein filament through which effector proteins are injected into eukaryotic host cells. Currently, the three-dimensional structure of the needle is unknown because it is not amenable to X-ray crystallography and solution NMR, as a result of its inherent non-crystallinity and insolubility. Cryo-electron microscopy combined with crystal or solution NMR subunit structures has recently provided a powerful hybrid approach for studying supramolecular assemblies, resulting in low-resolution and medium-resolution models. However, such approaches cannot deliver atomic details, especially of the crucial subunit-subunit interfaces, because of the limited cryo-electron microscopic resolution obtained in these studies. Here we report an alternative approach combining recombinant wild-type needle production, solid-state NMR, electron microscopy and Rosetta modelling to reveal the supramolecular interfaces and ultimately the complete atomic structure of the Salmonella typhimurium T3SS needle. We show that the 80-residue subunits form a right-handed helical assembly with roughly 11 subunits per two turns, similar to that of the flagellar filament of S. typhimurium. In contrast to established models of the needle in which the amino terminus of the protein subunit was assumed to be alpha-helical and positioned inside the needle, our model reveals an extended amino-terminal domain that is positioned on the surface of the needle, while the highly conserved carboxy terminus points towards the lumen.
Atomic model of the type III secretion system needle.,Loquet A, Sgourakis NG, Gupta R, Giller K, Riedel D, Goosmann C, Griesinger C, Kolbe M, Baker D, Becker S, Lange A Nature. 2012 May 20;486(7402):276-9. doi: 10.1038/nature11079. PMID:22699623[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Loquet A, Sgourakis NG, Gupta R, Giller K, Riedel D, Goosmann C, Griesinger C, Kolbe M, Baker D, Becker S, Lange A. Atomic model of the type III secretion system needle. Nature. 2012 May 20;486(7402):276-9. doi: 10.1038/nature11079. PMID:22699623 doi:10.1038/nature11079
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