|
|
Line 3: |
Line 3: |
| <SX load='6pee' size='340' side='right' viewer='molstar' caption='[[6pee]], [[Resolution|resolution]] 3.42Å' scene=''> | | <SX load='6pee' size='340' side='right' viewer='molstar' caption='[[6pee]], [[Resolution|resolution]] 3.42Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6pee]] is a 15 chain structure with sequence from [http://en.wikipedia.org/wiki/Salty Salty]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PEE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6PEE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6pee]] is a 15 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=6PEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PEE FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene></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]] 3.42Å</td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6pee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pee OCA], [http://pdbe.org/6pee PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pee RCSB], [http://www.ebi.ac.uk/pdbsum/6pee PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pee ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene></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=6pee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pee OCA], [https://pdbe.org/6pee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pee RCSB], [https://www.ebi.ac.uk/pdbsum/6pee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pee ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://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;">
| + | |
- | == Publication Abstract from PubMed ==
| + | |
- | The bacterial injectisome is a syringe-shaped macromolecular nanomachine utilized by many pathogenic Gram-negative bacteria, including the causative agents of plague, typhoid fever, whooping cough, sexually transmitted infections and major nosocomial infections. Bacterial proteins destined for self-assembly and host-cell targeting are translocated by the injectisome in a process known as type III secretion (T3S). The core structure is the ~4 MDa needle complex (NC), built on a foundation of three highly oligomerized ring-forming proteins that create a hollow scaffold spanning the bacterial inner membrane (IM) (24-mer ring-forming proteins PrgH and PrgK in the Salmonella enterica serovar Typhimurium Salmonella pathogenicity island 1 (SPI-1) type III secretion system (T3SS)) and outer membrane (OM) (15-mer InvG, a member of the broadly conserved secretin pore family). An internalized helical needle projects from the NC and bacterium, ultimately forming a continuous passage to the host, for delivery of virulence effectors. Here, we have captured snapshots of the entire prototypical SPI-1 NC in four distinct needle assembly states, including near-atomic resolution, and local reconstructions in the absence and presence of the needle. These structures reveal the precise localization and molecular interactions of the internalized SpaPQR 'export apparatus' complex, which is intimately encapsulated and stabilized within the IM rings in the manner of a nanodisc, and to which the PrgJ rod directly binds and functions as an initiator and anchor of needle polymerization. We also describe the molecular details of the extensive and continuous coupling interface between the OM secretin and IM rings, which is remarkably facilitated by a localized 16-mer stoichiometry in the periplasmic-most coupling domain of the otherwise 15-mer InvG oligomer.
| + | |
- | | + | |
- | T3S injectisome needle complex structures in four distinct states reveal the basis of membrane coupling and assembly.,Hu J, Worrall LJ, Vuckovic M, Hong C, Deng W, Atkinson CE, Brett Finlay B, Yu Z, Strynadka NCJ Nat Microbiol. 2019 Aug 19. pii: 10.1038/s41564-019-0545-z. doi:, 10.1038/s41564-019-0545-z. PMID:31427728<ref>PMID:31427728</ref>
| + | |
- | | + | |
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
- | </div> | + | |
- | <div class="pdbe-citations 6pee" style="background-color:#fffaf0;"></div> | + | |
| == References == | | == References == |
| <references/> | | <references/> |
Line 23: |
Line 15: |
| </SX> | | </SX> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Salty]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]] |
- | [[Category: Hu, J]] | + | [[Category: Hu J]] |
- | [[Category: Strynadka, N C.J]] | + | [[Category: Strynadka NCJ]] |
- | [[Category: Worrall, L J]] | + | [[Category: Worrall LJ]] |
- | [[Category: Bacterial secretion]]
| + | |
- | [[Category: Outer membrane]]
| + | |
- | [[Category: Protein transport]]
| + | |
- | [[Category: Secretin]]
| + | |
- | [[Category: Type iii secretion]]
| + | |
| 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]
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
|