1m0v
From Proteopedia
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|PDB= 1m0v |SIZE=350|CAPTION= <scene name='initialview01'>1m0v</scene> | |PDB= 1m0v |SIZE=350|CAPTION= <scene name='initialview01'>1m0v</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m0v OCA], [http://www.ebi.ac.uk/pdbsum/1m0v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m0v RCSB]</span> | ||
}} | }} | ||
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[[Category: Smith, C L.]] | [[Category: Smith, C L.]] | ||
[[Category: Zuiderweg, E R.P.]] | [[Category: Zuiderweg, E R.P.]] | ||
| - | [[Category: ACE]] | ||
| - | [[Category: NH2]] | ||
[[Category: high resolution structure]] | [[Category: high resolution structure]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:09:52 2008'' |
Revision as of 19:09, 30 March 2008
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| Ligands: | , , | ||||||
| Activity: | Protein-tyrosine-phosphatase, with EC number 3.1.3.48 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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