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1kdl

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==Solution structure of the amphipathic domain of YopD from Yersinia==
==Solution structure of the amphipathic domain of YopD from Yersinia==
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<StructureSection load='1kdl' size='340' side='right'caption='[[1kdl]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
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<StructureSection load='1kdl' size='340' side='right'caption='[[1kdl]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1kdl]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KDL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KDL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1kdl]] 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=1KDL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KDL FirstGlance]. <br>
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</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=1kdl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kdl OCA], [http://pdbe.org/1kdl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kdl RCSB], [http://www.ebi.ac.uk/pdbsum/1kdl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kdl ProSAT]</span></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kdl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kdl OCA], [https://pdbe.org/1kdl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kdl RCSB], [https://www.ebi.ac.uk/pdbsum/1kdl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kdl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/YOPD_YERPS YOPD_YERPS]] Interacts with the target membrane to form channel structures involved either in translocation of YopE into the cytoplasmic space of the target cell or in the cytotoxic effect of the YopE protein.
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[https://www.uniprot.org/uniprot/YOPD_YERPS YOPD_YERPS] Interacts with the target membrane to form channel structures involved either in translocation of YopE into the cytoplasmic space of the target cell or in the cytotoxic effect of the YopE protein.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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To establish an infection, Yersinia pseudotuberculosis utilizes a plasmid-encoded type III secretion machine that permits the translocation of several anti-host factors into the cytosol of target eukaryotic cells. Secreted YopD is essential for this process. Pre-secretory stabilization of YopD is mediated by an interaction with its cognate chaperone, LcrH. YopD possesses LcrH binding domains located in the N-terminus and in a predicted amphipathic domain located near the C-terminus. This latter domain is also critical for Yersinia virulence. In this study, we designed synthetic peptides encompassing the C-terminal amphipathic domain of YopD. A solution structure of YopD278-300, a peptide that strongly interacted with LcrH, was obtained by NMR methods. The structure is composed of a well-defined amphipathic alpha helix ranging from Phe280 to Tyr291, followed by a type I beta turn between residues Val292 and His295. The C-terminal truncated peptides, YopD278-292 and YopD271-292, lacked helical structure, implicating the beta turn in helix stability. An interaction between YopD278-300 and its cognate chaperone, LcrH, was observed by NMR through line-broadening effects and chemical shift differences between the free peptide and the peptide-LcrH complex. These effects were not observed for the unstructured peptide, YopD278-292, which confirms that the alpha helical structure of the YopD amphipathic domain is a critical binding region of LcrH.
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Conformational analysis by CD and NMR spectroscopy of a peptide encompassing the amphipathic domain of YopD from Yersinia.,Tengel T, Sethson I, Francis MS Eur J Biochem. 2002 Aug;269(15):3659-68. PMID:12153562<ref>PMID:12153562</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 1kdl" 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: Francis, M S]]
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[[Category: Yersinia pseudotuberculosis IP 32953]]
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[[Category: Sethson, I]]
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[[Category: Francis MS]]
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[[Category: Tengel, T]]
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[[Category: Sethson I]]
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[[Category: Amphipathic alpha helix]]
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[[Category: Tengel T]]
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[[Category: Beta turn]]
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[[Category: Structural protein]]
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[[Category: Yersinia]]
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[[Category: Yopd]]
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Current revision

Solution structure of the amphipathic domain of YopD from Yersinia

PDB ID 1kdl

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