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[[Image:1m0v.jpg|left|200px]]
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{{STRUCTURE_1m0v|  PDB=1m0v  |  SCENE=  }}
'''NMR STRUCTURE OF THE TYPE III SECRETORY DOMAIN OF YERSINIA YOPH COMPLEXED WITH THE SKAP-HOM PHOSPHO-PEPTIDE N-acetyl-DEpYDDPF-NH2'''


==NMR STRUCTURE OF THE TYPE III SECRETORY DOMAIN OF YERSINIA YOPH COMPLEXED WITH THE SKAP-HOM PHOSPHO-PEPTIDE N-acetyl-DEpYDDPF-NH2==
<StructureSection load='1m0v' size='340' side='right'caption='[[1m0v]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1m0v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Yersinia_pseudotuberculosis Yersinia pseudotuberculosis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M0V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M0V FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m0v OCA], [https://pdbe.org/1m0v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m0v RCSB], [https://www.ebi.ac.uk/pdbsum/1m0v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m0v ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/YOPH_YERPS YOPH_YERPS] Essential virulence determinant. This protein is a protein tyrosine phosphatase. The essential function of YopH in Yersinia pathogenesis is host-protein dephosphorylation. It contributes to the ability of the bacteria to resist phagocytosis by peritoneal macrophages.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:12234185</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1M0V is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Yersinia_pseudotuberculosis Yersinia pseudotuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M0V OCA].
</div>
<div class="pdbe-citations 1m0v" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/12234185 12234185]
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
[[Category: Protein complex]]
== References ==
[[Category: Protein-tyrosine-phosphatase]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Yersinia pseudotuberculosis]]
[[Category: Yersinia pseudotuberculosis]]
[[Category: Keliikuli, K.]]
[[Category: Keliikuli K]]
[[Category: Khandelwal, P.]]
[[Category: Khandelwal P]]
[[Category: Saper, M A.]]
[[Category: Saper MA]]
[[Category: Smith, C L.]]
[[Category: Smith CL]]
[[Category: Zuiderweg, E R.P.]]
[[Category: Zuiderweg ERP]]
[[Category: High resolution structure]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:29:45 2008''

Latest revision as of 00:14, 21 November 2024

NMR STRUCTURE OF THE TYPE III SECRETORY DOMAIN OF YERSINIA YOPH COMPLEXED WITH THE SKAP-HOM PHOSPHO-PEPTIDE N-acetyl-DEpYDDPF-NH2

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