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New page: left|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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[[Image:1m0v.jpg|left|200px]]<br /><applet load="1m0v" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1m0v.jpg|left|200px]]<br /><applet load="1m0v" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1m0v" />
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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'''<br />
'''NMR STRUCTURE OF THE TYPE III SECRETORY DOMAIN OF YERSINIA YOPH COMPLEXED WITH THE SKAP-HOM PHOSPHO-PEPTIDE N-acetyl-DEpYDDPF-NH2'''<br />


==Overview==
==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.
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==
==About this Structure==
1M0V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Yersinia_pseudotuberculosis Yersinia pseudotuberculosis] with ACE and NH2 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M0V OCA].  
1M0V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Yersinia_pseudotuberculosis Yersinia pseudotuberculosis] with <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M0V OCA].  


==Reference==
==Reference==
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[[Category: Keliikuli, K.]]
[[Category: Keliikuli, K.]]
[[Category: Khandelwal, P.]]
[[Category: Khandelwal, P.]]
[[Category: Saper, M.A.]]
[[Category: Saper, M A.]]
[[Category: Smith, C.L.]]
[[Category: Smith, C L.]]
[[Category: Zuiderweg, E.R.P.]]
[[Category: Zuiderweg, E R.P.]]
[[Category: ACE]]
[[Category: ACE]]
[[Category: NH2]]
[[Category: NH2]]
[[Category: high resolution structure]]
[[Category: high resolution structure]]


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