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PDBsum entry 1jln

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protein links
Hydrolase PDB id
1jln
Jmol
Contents
Protein chain
297 a.a. *
Waters ×238
* Residue conservation analysis
PDB id:
1jln
Name: Hydrolase
Title: Crystal structure of the catalytic domain of protein tyrosine phosphatase ptp-sl/br7
Structure: Protein tyrosine phosphatase, receptor type, r. Chain: a. Fragment: catalytic domain. Synonym: step-like ptpase. Protein-tyrosine-phosphatase receptor type ptpbr7. Ptpbr7. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.81Å     R-factor:   0.195     R-free:   0.245
Authors: S.E.Szedlacsek,A.R.Aricescu,T.A.Fulga,L.Renault,A.J.Scheidig
Key ref:
S.E.Szedlacsek et al. (2001). Crystal structure of PTP-SL/PTPBR7 catalytic domain: implications for MAP kinase regulation. J Mol Biol, 311, 557-568. PubMed id: 11493009 DOI: 10.1006/jmbi.2001.4890
Date:
16-Jul-01     Release date:   17-Aug-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q62132  (PTPRR_MOUSE) -  Receptor-type tyrosine-protein phosphatase R
Seq:
Struc:
 
Seq:
Struc:
656 a.a.
297 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 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
+ 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     dephosphorylation   2 terms 
  Biochemical function     phosphatase activity     2 terms  

 

 
    reference    
 
 
DOI no: 10.1006/jmbi.2001.4890 J Mol Biol 311:557-568 (2001)
PubMed id: 11493009  
 
 
Crystal structure of PTP-SL/PTPBR7 catalytic domain: implications for MAP kinase regulation.
S.E.Szedlacsek, A.R.Aricescu, T.A.Fulga, L.Renault, A.J.Scheidig.
 
  ABSTRACT  
 
Protein tyrosine phosphatases PTP-SL and PTPBR7 are isoforms belonging to cytosolic membrane-associated and to receptor-like PTPs (RPTPs), respectively. They represent a new family of PTPs with a major role in activation and translocation of MAP kinases. Specifically, the complex formation between PTP-SL and ERK2 involves an unusual interaction leading to the phosphorylation of PTP-SL by ERK2 at Thr253 and the inactivating dephosphorylation of ERK2 by PTP-SL. This interaction is strictly dependent upon a kinase interaction motif (KIM) (residues 224-239) situated at the N terminus of the PTP-SL catalytic domain. We report the first crystal structure of the catalytic domain for a member of this family (PTP-SL, residues 254-549, identical with residues 361-656 of PTPBR7), providing an example of an RPTP with single cytoplasmic domain, which is monomeric, having an unhindered catalytic site. In addition to the characteristic PTP-core structure, PTP-SL has an N-terminal helix, possibly orienting the KIM motif upon interaction with the target ERK2. An unusual residue in the catalytically important WPD loop promotes formation of a hydrophobically and electrostatically stabilised clamp. This could induce increased rigidity to the WPD loop and therefore reduced catalytic activity, in agreement with our kinetic measurements. A docking model based on the PTP-SL structure suggests that, in the complex with ERK2, the phosphorylation of PTP-SL should be accomplished first. The subsequent dephosphorylation of ERK2 seems to be possible only if a conformational rearrangement of the two interacting partners takes place.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. Three-dimensional structure of RPTP-SL/BR7. Secondary structure elements were determined by the program DSSP[52], using the nomenclature given by Barford et al[17]. Helix a0 (residues 256-265) is represented in green while all other helices are in blue. All b-strands are represented in red. The movable WPD-loop, the active-site cysteine residue Cys480 and the phosphorylation site Ser/Thr253 are highlighted in green.
Figure 4.
Figure 4. The N-terminal helix a0. (a) Stereo view of the final 2F[o] -F[c] electron density map contoured at the 1.5s level. The refined model (ball-and-stick) is superimposed, displaying the residues 256 to 265. (b) Stereodiagram showing the main interactions of helix a0 with the PTP domain. Only specifically conserved residues of the KIM-containing PTPs family are represented. Residues of helix a0 are in green, those of helix a5 are in blue and those of the loop between Ile292 and Asp298 are in magenta.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (2001, 311, 557-568) copyright 2001.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19424502 M.C.Balasu, L.N.Spiridon, S.Miron, C.T.Craescu, A.J.Scheidig, A.J.Petrescu, and S.E.Szedlacsek (2009).
Interface analysis of the complex between ERK2 and PTP-SL.
  PLoS ONE, 4, e5432.  
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
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.  
17532515 A.C.Bishop, X.Y.Zhang, and A.M.Lone (2007).
Generation of inhibitor-sensitive protein tyrosine phosphatases via active-site mutations.
  Methods, 42, 278-288.  
17596826 A.K.Nordle, P.Rios, A.Gaulton, R.Pulido, T.K.Attwood, and L.Tabernero (2007).
Functional assignment of MAPK phosphatase domains.
  Proteins, 69, 19-31.  
16919785 A.J.Barr, and S.Knapp (2006).
MAPK-specific tyrosine phosphatases: new targets for drug discovery?
  Trends Pharmacol Sci, 27, 525-530.  
15333922 A.K.Pedersen, G.H.Peters G, K.B.Møller, L.F.Iversen, and J.S.Kastrup (2004).
Water-molecule network and active-site flexibility of apo protein tyrosine phosphatase 1B.
  Acta Crystallogr D Biol Crystallogr, 60, 1527-1534.
PDB code: 1sug
15466470 Z.Huang, B.Zhou, and Z.Y.Zhang (2004).
Molecular determinants of substrate recognition in hematopoietic protein-tyrosine phosphatase.
  J Biol Chem, 279, 52150-52159.  
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.