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| [[Image:1k46.gif|left|200px]]<br /><applet load="1k46" size="450" color="white" frame="true" align="right" spinBox="true"
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| caption="1k46, resolution 2.20Å" />
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| '''Crystal Structure of the Type III Secretory Domain of Yersinia YopH Reveals a Domain-Swapped Dimer'''<br />
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| ==Overview== | | ==Crystal Structure of the Type III Secretory Domain of Yersinia YopH Reveals a Domain-Swapped Dimer== |
| 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.
| | <StructureSection load='1k46' size='340' side='right'caption='[[1k46]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == |
| | <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> |
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</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> |
| | == 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. |
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| ==About this Structure== | | ==See Also== |
| 1K46 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_pseudotuberculosis Yersinia pseudotuberculosis]. 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=1K46 OCA].
| | *[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]] |
| | | __TOC__ |
| ==Reference==
| | </StructureSection> |
| 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11737640 11737640]
| | [[Category: Large Structures]] |
| [[Category: Protein-tyrosine-phosphatase]]
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| [[Category: Single protein]] | |
| [[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: domain-swap]]
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| [[Category: phosphopeptide-binding domain]]
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| [[Category: type iii secretion domain]]
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| ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:50:39 2007''
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