6rwk

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==MxiD N0 N1 and MxiG C-terminal domains of the Shigella type 3 secretion system==
==MxiD N0 N1 and MxiG C-terminal domains of the Shigella type 3 secretion system==
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<StructureSection load='6rwk' size='340' side='right'caption='[[6rwk]], [[Resolution|resolution]] 3.86&Aring;' scene=''>
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<SX load='6rwk' size='340' side='right' viewer='molstar' caption='[[6rwk]], [[Resolution|resolution]] 3.86&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6rwk]] is a 32 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=6RWK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RWK FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6rwk]] is a 32 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=6RWK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RWK FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6rwx|6rwx]], [[6rwy|6rwy]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.86&#8491;</td></tr>
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<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=6rwk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rwk OCA], [http://pdbe.org/6rwk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rwk RCSB], [http://www.ebi.ac.uk/pdbsum/6rwk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rwk ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6rwk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rwk OCA], [https://pdbe.org/6rwk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rwk RCSB], [https://www.ebi.ac.uk/pdbsum/6rwk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rwk ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MXID_SHIFL MXID_SHIFL]] Necessary for the secretion of IPA invasins. [[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.
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[https://www.uniprot.org/uniprot/SCTC_SHIFL SCTC_SHIFL] Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:8437520). Forms a ring-shaped multimeric structure with an apparent central pore in the outer membrane (PubMed:11717255). Necessary for the secretion of Ipa invasins (PubMed:8437520).<ref>PMID:11717255</ref> <ref>PMID:8437520</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:32092125</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6rwk" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Shigella flexneri]]
[[Category: Shigella flexneri]]
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[[Category: Kamprad, A]]
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[[Category: Kamprad A]]
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[[Category: Lunelli, M]]
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[[Category: Lunelli M]]
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[[Category: Beta-sheet augmentation]]
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[[Category: Protein transport]]
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[[Category: Secretin]]
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[[Category: Shigella]]
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[[Category: Type 3 secretion system]]
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Current revision

MxiD N0 N1 and MxiG C-terminal domains of the Shigella type 3 secretion system

6rwk, resolution 3.86Å

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