2xxs: Difference between revisions
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New page: '''Unreleased structure''' The entry 2xxs is ON HOLD Authors: McDowell, M.A., Johnson, S., Deane, J.E., McDonnell, J.M., Lea, S.M. Description: Solution structure of the N-terminal dom... |
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The | ==Solution structure of the N-terminal domain of the Shigella type III secretion protein MxiG== | ||
<StructureSection load='2xxs' size='340' side='right'caption='[[2xxs]]' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=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> | |||
</table> | |||
== Function == | |||
[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;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2xxs" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Shigella flexneri]] | |||
[[Category: Deane JE]] | |||
[[Category: Johnson S]] | |||
[[Category: Lea SM]] | |||
[[Category: McDonnell JM]] | |||
[[Category: McDowell MA]] | |||
Latest revision as of 14:01, 1 February 2024
Solution structure of the N-terminal domain of the Shigella type III secretion protein MxiG
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