1kdl: Difference between revisions
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{{STRUCTURE_1kdl| PDB=1kdl | SCENE= }} | |||
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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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==About this Structure== | ==About this Structure== | ||
1KDL is a [[Single protein]] structure | 1KDL is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KDL OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Sethson, I.]] | [[Category: Sethson, I.]] | ||
[[Category: Tengel, T.]] | [[Category: Tengel, T.]] | ||
[[Category: | [[Category: Amphipathic alpha helix]] | ||
[[Category: | [[Category: Beta turn]] | ||
[[Category: | [[Category: Yersinia]] | ||
[[Category: | [[Category: Yopd]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:36:41 2008'' | |||
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Revision as of 19:36, 2 May 2008
Solution structure of the amphipathic domain of YopD from Yersinia
Overview
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.
About this Structure
1KDL is a Single protein structure. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 22:36:41 2008
