1M0V
NMR STRUCTURE OF THE TYPE III SECRETORY DOMAIN OF YERSINIA YOPH COMPLEXED WITH THE SKAP-HOM PHOSPHO-PEPTIDE N-acetyl-DEpYDDPF-NH2
Summary for 1M0V
| Entry DOI | 10.2210/pdb1m0v/pdb |
| Descriptor | PROTEIN-TYROSINE PHOSPHATASE YOPH, SKAP55 homologue (2 entities in total) |
| Functional Keywords | high resolution structure, hydrolase |
| Biological source | Yersinia pseudotuberculosis More |
| Cellular location | Secreted: p08538 |
| Total number of polymer chains | 2 |
| Total formula weight | 15886.48 |
| Authors | Khandelwal, P.,Keliikuli, K.,Smith, C.L.,Saper, M.A.,Zuiderweg, E.R.P. (deposition date: 2002-06-14, release date: 2002-07-24, Last modification date: 2024-11-20) |
| Primary citation | Khandelwal, P.,Keliikuli, K.,Smith, C.L.,Saper, M.A.,Zuiderweg, E.R.P. Solution structure and phosphopeptide binding to the N-terminal domain of Yersinia YopH: comparison with a crystal structure Biochemistry, 41:11425-11437, 2002 Cited by PubMed Abstract: 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. PubMed: 12234185DOI: 10.1021/bi026333l PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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