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| | <StructureSection load='3uep' size='340' side='right'caption='[[3uep]], [[Resolution|resolution]] 2.25Å' scene=''> | | <StructureSection load='3uep' size='340' side='right'caption='[[3uep]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3uep]] is a 2 chain structure with sequence from [https://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=3UEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UEP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3uep]] 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=3UEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UEP FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pYV virulence plasmid, pYV0070, yscQ ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=633 "Bacillus pseudotuberkulosis" (sic) Pfeiffer 1889])</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]] 2.25Å</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=3uep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uep OCA], [https://pdbe.org/3uep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uep RCSB], [https://www.ebi.ac.uk/pdbsum/3uep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uep ProSAT]</span></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=3uep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uep OCA], [https://pdbe.org/3uep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uep RCSB], [https://www.ebi.ac.uk/pdbsum/3uep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uep ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/YSCQ_YERPS YSCQ_YERPS]] Component of the Yop secretion machinery.
| + | [https://www.uniprot.org/uniprot/YSCQ_YERPS YSCQ_YERPS] Component of the Yop secretion machinery. |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | The bacterial flagellar C-ring is composed of two essential proteins, FliM and FliN. The smaller protein, FliN, is similar to the C-terminus of the larger protein, FliM, both being composed of SpoA domains. While bacterial type III secretion (T3S) systems encode many proteins in common with the flagellum, they mostly have a single protein in place of FliM and FliN. This protein resembles FliM at its N-terminus and is as large as FliM but is more like FliN at its C-terminal SpoA domain. We have discovered that a FliN-sized cognate indeed exists in the Yersinia T3S system to accompany the FliM-sized cognate. The FliN-sized cognate, YscQ-C, is the product of an internal translation initiation site within the locus encoding the FliM-sized cognate YscQ. Both intact YscQ and YscQ-C were found to be required for T3S, indicating that the internal translation initiation site, which is conserved in some but not all YscQ orthologs, is crucial for function. The crystal structure of YscQ-C revealed a SpoA domain that forms a highly intertwined, domain-swapped homodimer, similar to those observed in FliN and the YscQ ortholog HrcQ(B). A single YscQ-C homodimer associated reversibly with a single molecule of intact YscQ, indicating conformational differences between the SpoA domains of intact YscQ and YscQ-C. A "snap-back" mechanism suggested by the structure can account for this. The 1:2 YscQ-YscQ-C complex is a close mimic of the 1:4 FliM-FliN complex and the likely building block of the putative Yersinia T3S system C-ring.
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| - | Two translation products of Yersinia yscQ assemble to form a complex essential to type III secretion.,Bzymek KP, Hamaoka BY, Ghosh P Biochemistry. 2012 Feb 28;51(8):1669-77. Epub 2012 Feb 15. PMID:22320351<ref>PMID:22320351</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 3uep" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bzymek, K P]] | + | [[Category: Yersinia pseudotuberculosis]] |
| - | [[Category: Ghosh, P]] | + | [[Category: Bzymek KP]] |
| - | [[Category: Cytosol]] | + | [[Category: Ghosh P]] |
| - | [[Category: Protein transport]]
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| - | [[Category: Type iii secretion protein]]
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