1y9t
From Proteopedia
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| - | [[Image:1y9t.jpg|left|200px]] | ||
| - | + | ==Crystal structure of a type III secretion system protein complexed with the lipid, 1-monohexanoyl-2-hydroxy-sn-glycero-3-phosphate== | |
| - | + | <StructureSection load='1y9t' size='340' side='right'caption='[[1y9t]], [[Resolution|resolution]] 1.87Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.87Å</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='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> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [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;"> | |
| - | == | + | == 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. | 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<ref>PMID:15775974</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1y9t" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Shigella flexneri]] | [[Category: Shigella flexneri]] | ||
| - | + | [[Category: Lario PI]] | |
| - | [[Category: Lario | + | [[Category: Strynadka NC]] |
| - | [[Category: Strynadka | + | |
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Current revision
Crystal structure of a type III secretion system protein complexed with the lipid, 1-monohexanoyl-2-hydroxy-sn-glycero-3-phosphate
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