1k46

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<StructureSection load='1k46' size='340' side='right'caption='[[1k46]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1k46' size='340' side='right'caption='[[1k46]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1k46]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_pseudotuberkulosis"_(sic)_pfeiffer_1889 "bacillus pseudotuberkulosis" (sic) pfeiffer 1889]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K46 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K46 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1k46]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pseudotuberculosis Yersinia pseudotuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K46 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K46 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1huf|1huf]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yopH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=633 "Bacillus pseudotuberkulosis" (sic) Pfeiffer 1889])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></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=1k46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k46 OCA], [https://pdbe.org/1k46 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k46 RCSB], [https://www.ebi.ac.uk/pdbsum/1k46 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k46 ProSAT]</span></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=1k46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k46 OCA], [https://pdbe.org/1k46 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k46 RCSB], [https://www.ebi.ac.uk/pdbsum/1k46 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k46 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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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[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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Pathogenic strains of Yersinia deploy a type III secretion system to inject the potent tyrosine phosphatase YopH into host cells, where it dephosphorylates focal adhesion-associated substrates. The amino-terminal, non-catalytic domain of YopH is bifunctional; it is essential for the secretion and binding of the specific chaperone SycH, but also targets the catalytic domain to substrates in the infected cell. We describe the 2.2 A resolution crystal structure of residues 1-129 of YopH from Yersinia pseudotuberculosis. The amino-terminal alpha-helix (2-17), comprising the secretion signal, and beta-strand (24-28) of one molecule exchange with another molecule to form a domain-swapped dimer. Nuclear magnetic resonance (NMR) and gel filtration experiments demonstrated that YopH(1-129) could exist as a monomer and/or a dimer in solution. The topology of the dimer and the dynamics of a monomeric form in solution observed by NMR imply that YopH has the propensity to unfold partially. The dimer is probably not important physiologically, but may mimic how SycH binds to the exposed non-polar surfaces of a partially unfolded YopH. Phosphopeptide-induced perturbations in NMR chemical shifts define a substrate-binding surface on YopH(1-129) that includes residues previously shown by mutagenesis to be essential for YopH function.
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Structure of the type III secretion and substrate-binding domain of Yersinia YopH phosphatase.,Smith CL, Khandelwal P, Keliikuli K, Zuiderweg ER, Saper MA Mol Microbiol. 2001 Nov;42(4):967-79. PMID:11737640<ref>PMID:11737640</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1k46" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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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: Keliikuli K]]
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[[Category: Khandelwal, P]]
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[[Category: Khandelwal P]]
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[[Category: Saper, M A]]
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[[Category: Saper MA]]
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[[Category: Smith, C L]]
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[[Category: Smith CL]]
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[[Category: Zuiderweg, E R.P]]
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[[Category: Zuiderweg ERP]]
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[[Category: Domain-swap]]
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[[Category: Hydrolase]]
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[[Category: Phosphopeptide-binding domain]]
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[[Category: Type iii secretion domain]]
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Current revision

Crystal Structure of the Type III Secretory Domain of Yersinia YopH Reveals a Domain-Swapped Dimer

PDB ID 1k46

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