PDBsum entry 1xxv

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Hydrolase PDB id
Protein chains
282 a.a. *
Waters ×297
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Yersinia yoph (residues 163-468) binds phosphonodifluorometh containing hexapeptide at two sites
Structure: Protein-tyrosine phosphatase yoph. Chain: a, b. Fragment: catalytic domain, residues 163-468. Synonym: virulence protein. Engineered: yes. Mutation: yes. Epidermal growth factor receptor derived peptide. Chain: c, d, e, f. Engineered: yes
Source: Yersinia enterocolitica. Organism_taxid: 630. Gene: yoph, yop51. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Other_details: chemically synthesized by robert zamboni and gresser, merck frosst, montreal
Biol. unit: Trimer (from PQS)
2.50Å     R-factor:   0.178     R-free:   0.229
Authors: M.I.Ivanov,J.A.Stuckey,H.L.Schubert,M.A.Saper,J.B.Bliska
Key ref: M.I.Ivanov et al. (2005). Two substrate-targeting sites in the Yersinia protein tyrosine phosphatase co-operate to promote bacterial virulence. Mol Microbiol, 55, 1346-1356. PubMed id: 15720545
08-Nov-04     Release date:   22-Mar-05    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P15273  (YOPH_YEREN) -  Tyrosine-protein phosphatase YopH
468 a.a.
282 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.  - Protein-tyrosine-phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Protein tyrosine phosphate + H2O = protein tyrosine + phosphate
Protein tyrosine phosphate
+ H(2)O
protein tyrosine
Bound ligand (Het Group name = FTY)
matches with 45.83% similarity
+ phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     dephosphorylation   2 terms 
  Biochemical function     phosphatase activity     2 terms  


Mol Microbiol 55:1346-1356 (2005)
PubMed id: 15720545  
Two substrate-targeting sites in the Yersinia protein tyrosine phosphatase co-operate to promote bacterial virulence.
M.I.Ivanov, J.A.Stuckey, H.L.Schubert, M.A.Saper, J.B.Bliska.
YopH is a protein tyrosine phosphatase and an essential virulence determinant of the pathogenic bacterium Yersinia. Yersinia delivers YopH into infected host cells using a type III secretion mechanism. YopH dephosphorylates several focal adhesion proteins including p130Cas in human epithelial cells, resulting in disruption of focal adhesions and cell detachment from the extracellular matrix. How the C-terminal protein tyrosine phosphatase domain of YopH targets specific substrates such as p130Cas in the complex milieu of the host cell has not been fully elucidated. An N-terminal non-catalytic domain of YopH binds p130Cas in a phosphotyrosine-dependent manner and functions as a novel substrate-targeting site. The structure of the YopH protein tyrosine phosphatase domain bound to a model phosphopeptide substrate was solved and the resulting structure revealed a second substrate-targeting site ('site 2') within the catalytic domain. Site 2 binds to p130Cas in a phosphotyrosine-dependent manner, and co-operates with the N-terminal domain ('site 1') to promote efficient recognition of p130Cas by YopH in epithelial cells. The identification of two substrate-targeting sites in YopH that co-operate to promote epithelial cell detachment and bacterial virulence reinforces the importance of protein-protein interactions for determining protein tyrosine phosphatase specificity in vivo, and highlights the sophisticated nature of microbial pathogenicity factors.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21118379 M.Leone, E.Barile, R.Dahl, and M.Pellecchia (2011).
Design and NMR studies of cyclic peptides targeting the N-terminal domain of the protein tyrosine phosphatase YopH.
  Chem Biol Drug Des, 77, 12-19.  
20199604 A.J.Davis, D.A.Díaz, and J.Mecsas (2010).
A dominant-negative needle mutant blocks type III secretion of early but not late substrates in Yersinia.
  Mol Microbiol, 76, 236-259.  
19221593 la Puerta, A.G.Trinidad, M.del Carmen Rodríguez, J.Bogetz, M.Sánchez Crespo, T.Mustelin, A.Alonso, and Y.Bayón (2009).
Characterization of new substrates targeted by Yersinia tyrosine phosphatase YopH.
  PLoS ONE, 4, e4431.  
19053285 D.A.Critton, A.Tortajada, G.Stetson, W.Peti, and R.Page (2008).
Structural basis of substrate recognition by hematopoietic tyrosine phosphatase.
  Biochemistry, 47, 13336-13345.
PDB codes: 2hvl 2qdc 2qdm 2qdp 3d42 3d44
18299249 F.Shao (2008).
Biochemical functions of Yersinia type III effectors.
  Curr Opin Microbiol, 11, 21-29.  
18298793 L.Tabernero, A.R.Aricescu, E.Y.Jones, and S.E.Szedlacsek (2008).
Protein tyrosine phosphatases: structure-function relationships.
  FEBS J, 275, 867-882.  
18591234 Y.Zhang, J.Murtha, M.A.Roberts, R.M.Siegel, and J.B.Bliska (2008).
Type III secretion decreases bacterial and host survival following phagocytosis of Yersinia pseudotuberculosis by macrophages.
  Infect Immun, 76, 4299-4310.  
17071752 A.J.Davis, and J.Mecsas (2007).
Mutations in the Yersinia pseudotuberculosis type III secretion system needle protein, YscF, that specifically abrogate effector translocation into host cells.
  J Bacteriol, 189, 83-97.  
17074849 M.L.Fisher, C.Castillo, and J.Mecsas (2007).
Intranasal inoculation of mice with Yersinia pseudotuberculosis causes a lethal lung infection that is dependent on Yersinia outer proteins and PhoP.
  Infect Immun, 75, 429-442.  
17420232 V.Auerbuch, and R.R.Isberg (2007).
Growth of Yersinia pseudotuberculosis in mice occurs independently of Toll-like receptor 2 expression and induction of interleukin-10.
  Infect Immun, 75, 3561-3570.  
16622194 M.Miura, J.Terajima, H.Izumiya, J.Mitobe, T.Komano, and H.Watanabe (2006).
OspE2 of Shigella sonnei is required for the maintenance of cell architecture of bacterium-infected cells.
  Infect Immun, 74, 2587-2595.  
16698773 X.Hu, and C.E.Stebbins (2006).
Dynamics of the WPD loop of the Yersinia protein tyrosine phosphatase.
  Biophys J, 91, 948-956.  
16098211 C.E.Stebbins (2005).
Structural microbiology at the pathogen-host interface.
  Cell Microbiol, 7, 1227-1236.  
15847602 G.I.Viboud, and J.B.Bliska (2005).
Yersinia outer proteins: role in modulation of host cell signaling responses and pathogenesis.
  Annu Rev Microbiol, 59, 69-89.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.