1m0v
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(New page: 200px<br /><applet load="1m0v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m0v" /> '''NMR STRUCTURE OF THE TYPE III SECRETORY DOMA...)
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Revision as of 18:55, 20 November 2007
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NMR STRUCTURE OF THE TYPE III SECRETORY DOMAIN OF YERSINIA YOPH COMPLEXED WITH THE SKAP-HOM PHOSPHO-PEPTIDE N-acetyl-DEpYDDPF-NH2
Overview
Virulence of pathogenic bacteria of the genus Yersinia requires the, injection of six effector proteins into the cytoplasm of host cells. The, amino-terminal domain of one of these effectors, the tyrosine phosphatase, YopH, is essential for translocation of YopH, as well as for targeting it, to phosphotyrosine-containing substrates of the type pYxxP. We report the, high-resolution solution structure of the N-terminal domain (residues, 1-129) from the Yersinia pseudotuberculosis YopH (YopH-NT) in complex with, N-acetyl-DEpYDDPF-NH(2), a peptide derived from an in vivo protein, substrate. In contrast to the domain-swapped dimer observed in a crystal, structure of the same protein (Smith, C. L., Khandelwal, P., Keliikuli, K., Zuiderweg, E. R. P., and Saper, M. A. (2001) Mol. Microbiol. 42, 967-979), YopH-NT is monomeric in solution. The peptide binding site is, located on a beta-hairpin that becomes the crossover point in the dimer, structure. The binding site has several characteristics that are, reminiscent of SH2 domains, which also bind to pYxxP sequences.
About this Structure
1M0V is a Protein complex structure of sequences from Yersinia pseudotuberculosis with ACE and NH2 as ligands. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Full crystallographic information is available from OCA.
Reference
Solution structure and phosphopeptide binding to the N-terminal domain of Yersinia YopH: comparison with a crystal structure., Khandelwal P, Keliikuli K, Smith CL, Saper MA, Zuiderweg ER, Biochemistry. 2002 Sep 24;41(38):11425-37. PMID:12234185
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