From Proteopedia
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| - | [[Image:1kdl.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1kdl| PDB=1kdl | SCENE= }} | | {{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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| - | ==Overview==
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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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12153562}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12153562 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12153562}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1KDL is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KDL OCA]. | + | 1KDL is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KDL OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Yersinia]] | | [[Category: Yersinia]] |
| | [[Category: Yopd]] | | [[Category: Yopd]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:36:41 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:10:37 2008'' |
Revision as of 07:10, 2 July 2008
Template:STRUCTURE 1kdl
Solution structure of the amphipathic domain of YopD from Yersinia
Template:ABSTRACT PUBMED 12153562
About this Structure
1KDL is a Single protein structure. Full experimental 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 Wed Jul 2 10:10:37 2008
