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| | <StructureSection load='1y9t' size='340' side='right'caption='[[1y9t]], [[Resolution|resolution]] 1.87Å' scene=''> | | <StructureSection load='1y9t' size='340' side='right'caption='[[1y9t]], [[Resolution|resolution]] 1.87Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1y9t]] is a 1 chain structure with sequence from [http://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=1Y9T OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Y9T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1y9t]] 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=1Y9T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y9T FirstGlance]. <br> |
| | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=HHG:(2R)-2-HYDROXY-3-(PHOSPHONOOXY)PROPYL+HEXANOATE'>HHG</scene></td></tr> | | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=HHG:(2R)-2-HYDROXY-3-(PHOSPHONOOXY)PROPYL+HEXANOATE'>HHG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1y9l|1y9l]]</div></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=1y9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y9t OCA], [https://pdbe.org/1y9t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y9t RCSB], [https://www.ebi.ac.uk/pdbsum/1y9t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y9t ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mxiM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 "Shigella paradysenteriae" Weldin 1927])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1y9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y9t OCA], [http://pdbe.org/1y9t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y9t RCSB], [http://www.ebi.ac.uk/pdbsum/1y9t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y9t ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MXIM_SHIFL MXIM_SHIFL]] Involved in the secretion of the Ipa antigens. | + | [https://www.uniprot.org/uniprot/SCTG_SHIFL SCTG_SHIFL] Involved in the synthesis of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:10085046, PubMed:11717255). Pilot protein that is required for the proper localization of the secretin MxiD/SctC in the outer membrane (PubMed:11717255). Also influences both MxiD/SctC multimerization and stability (PubMed:11717255). Required for both Ipa translocation and tissue culture cell invasion (PubMed:10085046). Binds lipids (PubMed:15775974).<ref>PMID:10085046</ref> <ref>PMID:11717255</ref> <ref>PMID:15775974</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Shigella paradysenteriae weldin 1927]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lario, P I]] | + | [[Category: Shigella flexneri]] |
| - | [[Category: Strynadka, N C]] | + | [[Category: Lario PI]] |
| - | [[Category: Cracked b-barrel fold]] | + | [[Category: Strynadka NC]] |
| - | [[Category: Lipid binding protein]]
| + | |
| - | [[Category: Mixed alpha/beta]]
| + | |
| Structural highlights
Function
SCTG_SHIFL Involved in the synthesis of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:10085046, PubMed:11717255). Pilot protein that is required for the proper localization of the secretin MxiD/SctC in the outer membrane (PubMed:11717255). Also influences both MxiD/SctC multimerization and stability (PubMed:11717255). Required for both Ipa translocation and tissue culture cell invasion (PubMed:10085046). Binds lipids (PubMed:15775974).[1] [2] [3]
Publication Abstract from PubMed
The ability to translocate virulence proteins into host cells through a type III secretion apparatus (TTSS) is a hallmark of several Gram-negative pathogens including Shigella, Salmonella, Yersinia, Pseudomonas, and enteropathogenic Escherichia coli. In common with other types of bacterial secretion apparatus, the assembly of the TTSS complex requires the preceding formation of its integral outer membrane secretin ring component. We have determined at 1.5 A the structure of MxiM28-142, the Shigella pilot protein that is essential for the assembly and membrane association of the Shigella secretin, MxiD. This represents the first atomic structure of a secretin pilot protein from the several bacterial secretion systems containing an orthologous secretin component. A deep hydrophobic cavity is observed in the novel 'cracked barrel' structure of MxiM, providing a specific binding domain for the acyl chains of bacterial lipids, a proposal that is supported by our various lipid/MxiM complex structures. Isothermal titration analysis shows that the C-terminal domain of the secretin, MxiD525-570, hinders lipid binding to MxiM.
Structure and biochemical analysis of a secretin pilot protein.,Lario PI, Pfuetzner RA, Frey EA, Creagh L, Haynes C, Maurelli AT, Strynadka NC EMBO J. 2005 Mar 23;24(6):1111-21. Epub 2005 Mar 10. PMID:15775974[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schuch R, Maurelli AT. The mxi-Spa type III secretory pathway of Shigella flexneri requires an outer membrane lipoprotein, MxiM, for invasin translocation. Infect Immun. 1999 Apr;67(4):1982-91. doi: 10.1128/IAI.67.4.1982-1991.1999. PMID:10085046 doi:http://dx.doi.org/10.1128/IAI.67.4.1982-1991.1999
- ↑ Schuch R, Maurelli AT. MxiM and MxiJ, base elements of the Mxi-Spa type III secretion system of Shigella, interact with and stabilize the MxiD secretin in the cell envelope. J Bacteriol. 2001 Dec;183(24):6991-8. doi: 10.1128/JB.183.24.6991-6998.2001. PMID:11717255 doi:http://dx.doi.org/10.1128/JB.183.24.6991-6998.2001
- ↑ Lario PI, Pfuetzner RA, Frey EA, Creagh L, Haynes C, Maurelli AT, Strynadka NC. Structure and biochemical analysis of a secretin pilot protein. EMBO J. 2005 Mar 23;24(6):1111-21. Epub 2005 Mar 10. PMID:15775974 doi:7600610
- ↑ Lario PI, Pfuetzner RA, Frey EA, Creagh L, Haynes C, Maurelli AT, Strynadka NC. Structure and biochemical analysis of a secretin pilot protein. EMBO J. 2005 Mar 23;24(6):1111-21. Epub 2005 Mar 10. PMID:15775974 doi:7600610
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