4d3e

From Proteopedia

(Difference between revisions)

Current revision

Tetramer of IpaD, modified from 2J0O, fitted into negative stain electron microscopy reconstruction of the wild type tip complex from the type III secretion system of Shigella flexneri

4d3e, resolution 2.12Å

Structural highlights

4d3e is a 1 chain structure with sequence from Shigella flexneri 5a str. M90T. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 2.12Å
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IPAD_SHIFL Required for bacterial invasion of host cells. Controls IpaB and IpaC secretion, and the efficiency with which they are physically inserted into target cell membranes. These proteins are exported via TTSS to form a pore in the host membrane that allows the translocation of the other effectors into the host cytoplasm. Along with IpaB, is essential for both blocking secretion through the Mxi/Spa translocon in the absence of a secretion-inducing signal, and for controlling the level of secretion in the presence of this signal.^[1] ^[2]

Publication Abstract from PubMed

Type III secretion systems are found in many Gram-negative bacteria. They are activated by contact with eukaryotic cells and inject virulence proteins inside them. Host cell detection requires a protein complex located at the tip of the device's external injection needle. The Shigella tip complex (TC) is composed of IpaD, a hydrophilic protein, and IpaB, a hydrophobic protein, which later forms part of the injection pore in the host membrane. Here we used labelling and crosslinking methods to show that TCs from a DeltaipaB strain contain five IpaD subunits while the TCs from wild-type can also contain one IpaB and four IpaD subunits. Electron microscopy followed by single particle and helical image analysis was used to reconstruct three-dimensional images of TCs at approximately 20 A resolution. Docking of an IpaD crystal structure, constrained by the crosslinks observed, reveals that TC organisation is different from that of all previously proposed models. Our findings suggest new mechanisms for TC assembly and function. The TC is the only site within these secretion systems targeted by disease-protecting antibodies. By suggesting how these act, our work will allow improvement of prophylactic and therapeutic strategies.

Three-dimensional electron microscopy reconstruction and cysteine-mediated crosslinking provide a model of the type III secretion system needle tip complex.,Cheung M, Shen DK, Makino F, Kato T, Roehrich AD, Martinez-Argudo I, Walker ML, Murillo I, Liu X, Pain M, Brown J, Frazer G, Mantell J, Mina P, Todd T, Sessions RB, Namba K, Blocker AJ Mol Microbiol. 2014 Oct 29. doi: 10.1111/mmi.12843. PMID:25353930^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Menard R, Sansonetti P, Parsot C. The secretion of the Shigella flexneri Ipa invasins is activated by epithelial cells and controlled by IpaB and IpaD. EMBO J. 1994 Nov 15;13(22):5293-302. PMID:7957095
↑ Picking WL, Nishioka H, Hearn PD, Baxter MA, Harrington AT, Blocker A, Picking WD. IpaD of Shigella flexneri is independently required for regulation of Ipa protein secretion and efficient insertion of IpaB and IpaC into host membranes. Infect Immun. 2005 Mar;73(3):1432-40. PMID:15731041 doi:http://dx.doi.org/10.1128/IAI.73.3.1432-1440.2005
↑ Cheung M, Shen DK, Makino F, Kato T, Roehrich AD, Martinez-Argudo I, Walker ML, Murillo I, Liu X, Pain M, Brown J, Frazer G, Mantell J, Mina P, Todd T, Sessions RB, Namba K, Blocker AJ. Three-dimensional electron microscopy reconstruction and cysteine-mediated crosslinking provide a model of the type III secretion system needle tip complex. Mol Microbiol. 2014 Oct 29. doi: 10.1111/mmi.12843. PMID:25353930 doi:http://dx.doi.org/10.1111/mmi.12843

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4d3e"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[4d3e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_flexneri_5a_str._M90T Shigella flexneri 5a str. M90T]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D3E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D3E FirstGlance]. <br>
-</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=4d3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d3e OCA], [https://pdbe.org/4d3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d3e RCSB], [https://www.ebi.ac.uk/pdbsum/4d3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d3e ProSAT]</span></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]] 2.12&#8491;</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=4d3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d3e OCA], [https://pdbe.org/4d3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d3e RCSB], [https://www.ebi.ac.uk/pdbsum/4d3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d3e ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/IPAD_SHIFL IPAD_SHIFL]] Required for bacterial invasion of host cells. Controls IpaB and IpaC secretion, and the efficiency with which they are physically inserted into target cell membranes. These proteins are exported via TTSS to form a pore in the host membrane that allows the translocation of the other effectors into the host cytoplasm. Along with IpaB, is essential for both blocking secretion through the Mxi/Spa translocon in the absence of a secretion-inducing signal, and for controlling the level of secretion in the presence of this signal.<ref>PMID:7957095</ref> <ref>PMID:15731041</ref>
+[https://www.uniprot.org/uniprot/IPAD_SHIFL IPAD_SHIFL] Required for bacterial invasion of host cells. Controls IpaB and IpaC secretion, and the efficiency with which they are physically inserted into target cell membranes. These proteins are exported via TTSS to form a pore in the host membrane that allows the translocation of the other effectors into the host cytoplasm. Along with IpaB, is essential for both blocking secretion through the Mxi/Spa translocon in the absence of a secretion-inducing signal, and for controlling the level of secretion in the presence of this signal.<ref>PMID:7957095</ref> <ref>PMID:15731041</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4d3e

From Proteopedia

Current revision

Tetramer of IpaD, modified from 2J0O, fitted into negative stain electron microscopy reconstruction of the wild type tip complex from the type III secretion system of Shigella flexneri

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox