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2ml9

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==Solution structure of YSCUCN in a micellar complex with SDS==
==Solution structure of YSCUCN in a micellar complex with SDS==
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<StructureSection load='2ml9' size='340' side='right'caption='[[2ml9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2ml9' size='340' side='right'caption='[[2ml9]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2ml9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Yerps Yerps]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ML9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ML9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2ml9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pseudotuberculosis_IP_32953 Yersinia pseudotuberculosis IP 32953]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ML9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ML9 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2jli|2jli]], [[2v5g|2v5g]], [[3bzl|3bzl]], [[3bzv|3bzv]], [[3c01|3c01]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pYV0074, yscU ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273123 YERPS])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ml9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ml9 OCA], [https://pdbe.org/2ml9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ml9 RCSB], [https://www.ebi.ac.uk/pdbsum/2ml9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ml9 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=2ml9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ml9 OCA], [https://pdbe.org/2ml9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ml9 RCSB], [https://www.ebi.ac.uk/pdbsum/2ml9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ml9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/YSCU_YERPS YSCU_YERPS]] Component of the yop secretion machinery.
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[https://www.uniprot.org/uniprot/YSCU_YERPS YSCU_YERPS] Component of the yop secretion machinery.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The inner membrane of Gram-negative bacteria is negatively charged, rendering positively charged cytoplasmic proteins in close proximity likely candidates for protein-membrane interactions. YscU is a Yersinia pseudotuberculosis type III secretion system protein crucial for bacterial pathogenesis. The protein contains a highly conserved positively charged linker sequence that separates membrane-spanning and cytoplasmic (YscUC) domains. Although disordered in solution, inspection of the primary sequence of the linker reveals that positively charged residues are separated with a typical helical periodicity. Here, we demonstrate that the linker sequence of YscU undergoes a largely electrostatically driven coil-to-helix transition upon binding to negatively charged membrane interfaces. Using membrane-mimicking sodium dodecyl sulfate micelles, an NMR derived structural model reveals the induction of three helical segments in the linker. The overall linker placement in sodium dodecyl sulfate micelles was identified by NMR experiments including paramagnetic relaxation enhancements. Partitioning of individual residues agrees with their hydrophobicity and supports an interfacial positioning of the helices. Replacement of positively charged linker residues with alanine resulted in YscUC variants displaying attenuated membrane-binding affinities, suggesting that the membrane interaction depends on positive charges within the linker. In vivo experiments with bacteria expressing these YscU replacements resulted in phenotypes displaying significantly reduced effector protein secretion levels. Taken together, our data identify a previously unknown membrane-interacting surface of YscUC that, when perturbed by mutations, disrupts the function of the pathogenic machinery in Yersinia.
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Negatively charged lipid membranes promote a disorder-order transition in the Yersinia YscU protein.,Weise CF, Login FH, Ho O, Grobner G, Wolf-Watz H, Wolf-Watz M Biophys J. 2014 Oct 21;107(8):1950-1961. doi: 10.1016/j.bpj.2014.09.005. PMID:25418176<ref>PMID:25418176</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2ml9" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Yerps]]
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[[Category: Yersinia pseudotuberculosis IP 32953]]
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[[Category: Weise, C F]]
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[[Category: Weise CF]]
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[[Category: Wolf-Watz, M]]
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[[Category: Wolf-Watz M]]
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[[Category: Membrane protein]]
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[[Category: Secretion specificity]]
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[[Category: Sodium dodecyl sulfate]]
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[[Category: Type iii secretion system]]
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[[Category: Yersinia]]
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[[Category: Yscu]]
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Current revision

Solution structure of YSCUCN in a micellar complex with SDS

PDB ID 2ml9

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