2xxs

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'''Unreleased structure'''
 
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The entry 2xxs is ON HOLD until Paper Publication
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==Solution structure of the N-terminal domain of the Shigella type III secretion protein MxiG==
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<StructureSection load='2xxs' size='340' side='right'caption='[[2xxs]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2xxs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XXS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XXS FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2xxs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xxs OCA], [https://pdbe.org/2xxs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xxs RCSB], [https://www.ebi.ac.uk/pdbsum/2xxs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xxs ProSAT]</span></td></tr>
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</table>
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== 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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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MxiG is a single-pass membrane protein that oligomerizes within the inner membrane ring of the Shigella flexneri type III secretion system (T3SS). The MxiG N-terminal domain (MxiG-N) is the predominant cytoplasmic structure; however, its role in T3SS assembly and secretion is largely uncharacterized. We have determined the solution structure of MxiG-N residues 6-112 (MxiG-N(6-112)), representing the first published structure of this T3SS domain. The structure shows strong structural homology to forkhead-associated (FHA) domains. Canonically, these cell-signaling modules bind phosphothreonine (Thr(P)) via highly conserved residues. However, the putative phosphate-binding pocket of MxiG-N(6-112) does not align with other FHA domain structures or interact with Thr(P). Furthermore, mutagenesis of potential phosphate-binding residues has no effect on S. flexneri T3SS assembly and function. Therefore, MxiG-N has a novel function for an FHA domain. Positioning of MxiG-N(6-112) within the EM density of the S. flexneri needle complex gives insight into the ambiguous stoichiometry of the T3SS, supporting models with 24 MxiG subunits in the inner membrane ring.
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Authors: McDowell, M.A., Johnson, S., Deane, J.E., McDonnell, J.M., Lea, S.M.
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Structural and Functional Studies on the N-terminal Domain of the Shigella Type III Secretion Protein MxiG.,McDowell MA, Johnson S, Deane JE, Cheung M, Roehrich AD, Blocker AJ, McDonnell JM, Lea SM J Biol Chem. 2011 Sep 2;286(35):30606-14. Epub 2011 Jul 5. PMID:21733840<ref>PMID:21733840</ref>
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Description: Solution structure of the N-terminal domain of the Shigella type III secretion protein MxiG
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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 2xxs" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Shigella flexneri]]
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[[Category: Deane JE]]
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[[Category: Johnson S]]
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[[Category: Lea SM]]
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[[Category: McDonnell JM]]
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[[Category: McDowell MA]]

Current revision

Solution structure of the N-terminal domain of the Shigella type III secretion protein MxiG

PDB ID 2xxs

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