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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[[Image:1m0v.jpg|left|200px]]<br /><applet load="1m0v" size="450" color="white" frame="true" align="right" spinBox="true"
 
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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 />
 
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==Overview==
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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==
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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.
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<StructureSection load='1m0v' size='340' side='right'caption='[[1m0v]]' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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<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>
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</table>
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== Function ==
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[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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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].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12234185 12234185]
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</div>
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[[Category: Protein complex]]
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<div class="pdbe-citations 1m0v" style="background-color:#fffaf0;"></div>
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[[Category: Protein-tyrosine-phosphatase]]
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[[Category: Yersinia pseudotuberculosis]]
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[[Category: Keliikuli, K.]]
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[[Category: Khandelwal, P.]]
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[[Category: Saper, M.A.]]
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[[Category: Smith, C.L.]]
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[[Category: Zuiderweg, E.R.P.]]
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[[Category: ACE]]
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[[Category: NH2]]
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[[Category: high resolution structure]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:03:03 2007''
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==See Also==
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*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Yersinia pseudotuberculosis]]
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[[Category: Keliikuli K]]
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[[Category: Khandelwal P]]
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[[Category: Saper MA]]
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[[Category: Smith CL]]
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[[Category: Zuiderweg ERP]]

Current revision

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

PDB ID 1m0v

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