PDBsum entry 1jln

Hydrolase

PDB id: 1jln

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

Protein chain

Q62132  (PTPRR_MOUSE) -  Receptor-type tyrosine-protein phosphatase R from Mus musculus

Seq: 656 a.a.

Struc: 297 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.1.3.48 - protein-tyrosine-phosphatase.
• Reaction: O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] + phosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Key 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.