4a4y

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Current revision (07:13, 1 May 2024) (edit) (undo)
 
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<StructureSection load='4a4y' size='340' side='right'caption='[[4a4y]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
<StructureSection load='4a4y' size='340' side='right'caption='[[4a4y]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4a4y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"shigella_paradysenteriae"_weldin_1927 "shigella paradysenteriae" weldin 1927]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A4Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A4Y FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4a4y]] is a 1 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=4A4Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A4Y FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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">X-ray diffraction, [[Resolution|Resolution]] 1.57&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2xxs|2xxs]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4a4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a4y OCA], [https://pdbe.org/4a4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a4y RCSB], [https://www.ebi.ac.uk/pdbsum/4a4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a4y 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=4a4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a4y OCA], [https://pdbe.org/4a4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a4y RCSB], [https://www.ebi.ac.uk/pdbsum/4a4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a4y ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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.
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[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Gram-negative bacteria use the type 3 secretion system (T3SS) to colonize host cells. T3SSs are ring-shaped macromolecular complexes specific for the transport of effector molecules into host cells. It was recently suggested that a cytosolic ring-shaped protein complex delivers effector molecules to the T3SS. However, how transport of effector proteins is regulated is not known. Here, we report the high-resolution X-ray crystal structure of the whole cytosolic domain of MxiG (MxiG(1-126)), a major component of the inner T3SS rings in Shigella flexneri. MxiG(1-126) folds as an FHA domain, which specifically binds phosphorylated threonines. Indeed, MxiG(1-126) binds to Spa33, a cytoplasmic-ring component of Shigella, as revealed in pulldown studies. Surface plasmon resonance analysis showed specific interaction of MxiG with a Spa33 peptide only if phosphorylated. In total, 24 copies of the MxiG(1-126) crystal structure were fitted into the cryo-EM map of the Shigella T3SS. The phosphoprotein binding site of each MxiG molecule faces the channel of the T3SS, allowing interaction with cytosolic binding partners. Secretion assays and host cell invasion studies of complemented Shigella knockout cells indicated that the phosphoprotein binding of MxiG is essential for bacterial virulence. Our findings suggest that MxiG is involved in T3SS regulation.-Barison, N., Lambers, J., Hurwitz, R., Kolbe, M. Interaction of MxiG with the cytosolic complex of the type III secretion system controls Shigella virulence.
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Interaction of MxiG with the cytosolic complex of the type III secretion system controls Shigella virulence.,Barison N, Lambers J, Hurwitz R, Kolbe M FASEB J. 2012 Jan 12. PMID:22247334<ref>PMID:22247334</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 4a4y" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Shigella paradysenteriae weldin 1927]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Barison, N]]
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[[Category: Shigella flexneri]]
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[[Category: Kolbe, M]]
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[[Category: Barison N]]
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[[Category: Fha domain]]
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[[Category: Kolbe M]]
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[[Category: Protein binding]]
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Current revision

Structure of the Cytosolic Domain of the Shigella T3SS component MxiG

PDB ID 4a4y

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