1KDL
Solution structure of the amphipathic domain of YopD from Yersinia
Summary for 1KDL
| Entry DOI | 10.2210/pdb1kdl/pdb |
| Descriptor | YOPD protein (1 entity in total) |
| Functional Keywords | yersinia, yopd, amphipathic alpha helix, beta turn, structural protein |
| Total number of polymer chains | 1 |
| Total formula weight | 2768.20 |
| Authors | Tengel, T.,Sethson, I.,Francis, M.S. (deposition date: 2001-11-13, release date: 2002-08-21, Last modification date: 2024-05-01) |
| Primary citation | Tengel, T.,Sethson, I.,Francis, M.S. Conformational analysis by CD and NMR spectroscopy of a peptide encompassing the amphipathic domain of YopD from Yersinia. Eur.J.Biochem., 269:3659-3668, 2002 Cited by PubMed Abstract: 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. PubMed: 12153562DOI: 10.1046/j.1432-1033.2002.03051.x PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
