View source for 2xxs


==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&reg;/PubMed&reg;, 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]]