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| | <SX load='6rwx' size='340' side='right' viewer='molstar' caption='[[6rwx]], [[Resolution|resolution]] 3.55Å' scene=''> | | <SX load='6rwx' size='340' side='right' viewer='molstar' caption='[[6rwx]], [[Resolution|resolution]] 3.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6rwx]] is a 48 chain structure with sequence from [http://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RWX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6RWX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6rwx]] is a 48 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RWX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RWX FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6rwk|6rwk]], [[6rwy|6rwy]]</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]] 3.55Å</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=6rwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rwx OCA], [http://pdbe.org/6rwx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rwx RCSB], [http://www.ebi.ac.uk/pdbsum/6rwx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rwx 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=6rwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rwx OCA], [https://pdbe.org/6rwx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rwx RCSB], [https://www.ebi.ac.uk/pdbsum/6rwx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rwx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MXIG_SHIFL MXIG_SHIFL]] Involved in the secretion of the Ipa antigens. Involved in the intracellular dissemination of Shigella. Part of the Mxi-Spa secretion apparatus. [[http://www.uniprot.org/uniprot/MXIJ_SHIFL MXIJ_SHIFL]] Involved in the secretion of the Ipa antigens. | + | [https://www.uniprot.org/uniprot/MXIG_SHIFL MXIG_SHIFL] Involved in the secretion of the Ipa antigens. Involved in the intracellular dissemination of Shigella. Part of the Mxi-Spa secretion apparatus. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Shigella flexneri]] | | [[Category: Shigella flexneri]] |
| - | [[Category: Kamprad, A]] | + | [[Category: Kamprad A]] |
| - | [[Category: Lunelli, M]] | + | [[Category: Lunelli M]] |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Ring-forming membrane protein]]
| + | |
| - | [[Category: Shigella]]
| + | |
| - | [[Category: Type 3 secretion system]]
| + | |
| Structural highlights
Function
MXIG_SHIFL Involved in the secretion of the Ipa antigens. Involved in the intracellular dissemination of Shigella. Part of the Mxi-Spa secretion apparatus.
Publication Abstract from PubMed
The Type III Secretion Systems (T3SS) needle complex is a conserved syringe-shaped protein translocation nanomachine with a mass of about 3.5 MDa essential for the survival and virulence of many Gram-negative bacterial pathogens. This system is composed of a membrane-embedded basal body and an extracellular needle that deliver effector proteins into host cells. High-resolution structures of the T3SS from different organisms and infection stages are needed to understand the underlying molecular mechanisms of effector translocation. Here, we present the cryo-electron microscopy structure of the isolated Shigella T3SS needle complex. The inner membrane (IM) region of the basal body adopts 24-fold rotational symmetry and forms a channel system that connects the bacterial periplasm with the export apparatus cage. The secretin oligomer adopts a heterogeneous architecture with 16- and 15-fold cyclic symmetry in the periplasmic N-terminal connector and C-terminal outer membrane ring, respectively. Two out of three IM subunits bind the secretin connector via a beta-sheet augmentation. The cryo-EM map also reveals the helical architecture of the export apparatus core, the inner rod, the needle and their intervening interfaces.
Cryo-EM structure of the Shigella type III needle complex.,Lunelli M, Kamprad A, Burger J, Mielke T, Spahn CMT, Kolbe M PLoS Pathog. 2020 Feb 24;16(2):e1008263. doi: 10.1371/journal.ppat.1008263. PMID:32092125[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lunelli M, Kamprad A, Burger J, Mielke T, Spahn CMT, Kolbe M. Cryo-EM structure of the Shigella type III needle complex. PLoS Pathog. 2020 Feb 24;16(2):e1008263. doi: 10.1371/journal.ppat.1008263. PMID:32092125 doi:http://dx.doi.org/10.1371/journal.ppat.1008263
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