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1kdl
From Proteopedia
(New page: 200px<br /><applet load="1kdl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kdl" /> '''Solution structure of the amphipathic domain...) |
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| - | [[Image:1kdl.gif|left|200px]]<br /><applet load="1kdl" size=" | + | [[Image:1kdl.gif|left|200px]]<br /><applet load="1kdl" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1kdl" /> | caption="1kdl" /> | ||
'''Solution structure of the amphipathic domain of YopD from Yersinia'''<br /> | '''Solution structure of the amphipathic domain of YopD from Yersinia'''<br /> | ||
==Overview== | ==Overview== | ||
| - | To establish an infection, Yersinia pseudotuberculosis utilizes a | + | 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== | ==About this Structure== | ||
| - | 1KDL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1KDL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KDL OCA]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12153562 12153562] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12153562 12153562] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Francis, M | + | [[Category: Francis, M S.]] |
[[Category: Sethson, I.]] | [[Category: Sethson, I.]] | ||
[[Category: Tengel, T.]] | [[Category: Tengel, T.]] | ||
| Line 20: | Line 20: | ||
[[Category: yopd]] | [[Category: yopd]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:32:55 2008'' |
Revision as of 11:32, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 13:32:55 2008
