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| | ==Structure of the Type III Secretion System Protein== | | ==Structure of the Type III Secretion System Protein== |
| - | <StructureSection load='4d9v' size='340' side='right' caption='[[4d9v]], [[Resolution|resolution]] 2.52Å' scene=''> | + | <StructureSection load='4d9v' size='340' side='right'caption='[[4d9v]], [[Resolution|resolution]] 2.52Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4d9v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pseudotuberkulosis"_(sic)_pfeiffer_1889 "bacillus pseudotuberkulosis" (sic) pfeiffer 1889]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D9V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4d9v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pseudotuberculosis Yersinia pseudotuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D9V FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xxs|2xxs]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.519Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pYV0080, yscD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=633 "Bacillus pseudotuberkulosis" (sic) Pfeiffer 1889])</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=4d9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d9v OCA], [https://pdbe.org/4d9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d9v RCSB], [https://www.ebi.ac.uk/pdbsum/4d9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d9v ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d9v OCA], [http://pdbe.org/4d9v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d9v RCSB], [http://www.ebi.ac.uk/pdbsum/4d9v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d9v ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/Q663I6_YERPS Q663I6_YERPS] |
| - | The virulence of a large number of Gram-negative bacterial pathogens depends on the type III secretion (T3S) system, which transports select bacterial proteins into host cells. An essential component of the Yersinia T3S system is YscD, a single-pass inner membrane protein. We report here the 2.52 A resolution structure of the cytoplasmic domain of YscD, called YscDc. The structure confirms that YscDc consists of a forkhead-associated (FHA) fold, which in many but not all cases specifies binding to phosphothreonine. YscDc, however, lacks the structural properties associated with phosphothreonine-binding, and thus most likely interacts with partners in a phosphorylation-independent manner. Structural comparison highlighted two loop regions, L3 and L4, as potential sites of interactions. Alanine substitutions of L3 and L4 had no deleterious effects on protein structure or stability, but abrogated T3S in a dominant-negative manner. To gain insight into the function of L3 and L4, we identified proteins associated with YscD by affinity purification coupled to mass spectrometry. The lipoprotein YscJ was found associated with wild-type YscD, as was the effector YopH. Notably, the L3 and L4 substitution mutants interacted with more YopH than did wild-type YscD. These substitution mutants also interacted with SycH (the specific chaperone for YopH), the putative C-ring component YscQ, and the ruler component YscP, whereas wild-type YscD did not. These results suggest that substitutions in the L3 and L4 loops of YscD disrupted the dissociation of SycH from YopH, leading to the accumulation of a large protein complex that stalled the T3S apparatus.
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| - | The structure and interactions of the cytoplasmic domain of the Yersinia type III secretion protein YscD.,Gamez A, Mukerjea R, Alayyoubi M, Ghassemian M, Ghosh P J Bacteriol. 2012 Aug 31. PMID:22942247<ref>PMID:22942247</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 4d9v" style="background-color:#fffaf0;"></div>
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| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Gamez, A M]] | + | [[Category: Large Structures]] |
| - | [[Category: Ghosh, P]] | + | [[Category: Yersinia pseudotuberculosis]] |
| - | [[Category: Fha domain]] | + | [[Category: Gamez AM]] |
| - | [[Category: Type iii secretion protein]] | + | [[Category: Ghosh P]] |
| - | [[Category: Unknown function]]
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