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[[Image:1kdl.png|left|200px]]
==Solution structure of the amphipathic domain of YopD from Yersinia==
<StructureSection load='1kdl' size='340' side='right' caption='[[1kdl]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
== Structural highlights ==
<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>
</td></tr><tr><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://www.rcsb.org/pdb/explore.do?structureId=1kdl RCSB], [http://www.ebi.ac.uk/pdbsum/1kdl PDBsum]</span></td></tr>
<table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


{{STRUCTURE_1kdl|  PDB=1kdl  |  SCENE=  }}
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>


===Solution structure of the amphipathic domain of YopD from Yersinia===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_12153562}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[1kdl]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KDL OCA].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:012153562</ref><references group="xtra"/>
[[Category: Francis, M S.]]
[[Category: Francis, M S.]]
[[Category: Sethson, I.]]
[[Category: Sethson, I.]]
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