1kdl
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Revision as of 16:58, 20 November 2007
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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 of sequence from [1]. 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
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