spacer
spacer

PDBsum entry 1m0v

Go to PDB code: 
protein ligands links
Hydrolase PDB id
1m0v
Jmol
Contents
Protein chain
130 a.a.
Ligands
ACE-ASP-GLU-PTR-
ASP-ASP-PRO-PHE-
NH2
PDB id:
1m0v
Name: Hydrolase
Title: Nmr structure of the type iii secretory domain of yersinia yoph complexed with the skap-hom phospho-peptide n-acetyl- depyddpf-nh2
Structure: Protein-tyrosine phosphatase yoph. Chain: a. Fragment: amino-terminal domain (residues 1-129). Synonym: virulence protein. Engineered: yes. Skap55 homologue. Chain: b. Synonym: skap-hom peptide. Engineered: yes
Source: Yersinia pseudotuberculosis. Organism_taxid: 633. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: this peptide was chemically synthesized. It is naturally found in mus musculus (mouse).
NMR struc: 20 models
Authors: P.Khandelwal,K.Keliikuli,C.L.Smith,M.A.Saper,E.R.P.Zuiderweg
Key ref:
P.Khandelwal et al. (2002). Solution structure and phosphopeptide binding to the N-terminal domain of Yersinia YopH: comparison with a crystal structure. Biochemistry, 41, 11425-11437. PubMed id: 12234185 DOI: 10.1021/bi026333l
Date:
14-Jun-02     Release date:   24-Jul-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P08538  (YOPH_YERPS) -  Tyrosine-protein phosphatase YopH
Seq:
Struc:
468 a.a.
130 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.3.1.3.48  - Protein-tyrosine-phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Protein tyrosine phosphate + H2O = protein tyrosine + phosphate
Protein tyrosine phosphate
Bound ligand (Het Group name = PTR)
matches with 76.00% similarity
+ H(2)O
= protein tyrosine
+ phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     pathogenesis   2 terms 
  Biochemical function     protein tyrosine phosphatase activity     1 term  

 

 
    reference    
 
 
DOI no: 10.1021/bi026333l Biochemistry 41:11425-11437 (2002)
PubMed id: 12234185  
 
 
Solution structure and phosphopeptide binding to the N-terminal domain of Yersinia YopH: comparison with a crystal structure.
P.Khandelwal, K.Keliikuli, C.L.Smith, M.A.Saper, E.R.Zuiderweg.
 
  ABSTRACT  
 
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.
 

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.  
20877914 G.W.Buchko, G.Niemann, E.S.Baker, M.E.Belov, R.D.Smith, F.Heffron, J.N.Adkins, and J.E.McDermott (2010).
A multi-pronged search for a common structural motif in the secretion signal of Salmonella enterica serovar Typhimurium type III effector proteins.
  Mol Biosyst, 6, 2448-2458.  
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.  
15772084 M.A.Seeliger, M.Spichty, S.E.Kelly, M.Bycroft, S.M.Freund, M.Karplus, and L.S.Itzhaki (2005).
Role of conformational heterogeneity in domain swapping and adapter function of the Cks proteins.
  J Biol Chem, 280, 30448-30459.  
16262795 M.Duckely, C.Oomen, F.Axthelm, P.Van Gelder, G.Waksman, and A.Engel (2005).
The VirE1VirE2 complex of Agrobacterium tumefaciens interacts with single-stranded DNA and forms channels.
  Mol Microbiol, 58, 1130-1142.  
15720545 M.I.Ivanov, J.A.Stuckey, H.L.Schubert, M.A.Saper, and J.B.Bliska (2005).
Two substrate-targeting sites in the Yersinia protein tyrosine phosphatase co-operate to promote bacterial virulence.
  Mol Microbiol, 55, 1346-1356.
PDB codes: 1xxp 1xxv
15093830 H.Remaut, and G.Waksman (2004).
Structural biology of bacterial pathogenesis.
  Curr Opin Struct Biol, 14, 161-170.  
15590783 P.Ghosh (2004).
Process of protein transport by the type III secretion system.
  Microbiol Mol Biol Rev, 68, 771-795.  
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.