PDBsum entry 2c7s

Hydrolase

PDB id: 2c7s

Contents

Protein chain

289 a.a. *

Ligands

ACT

Waters ×138

* Residue conservation analysis

PDB id:

2c7s

Name:

Hydrolase

Title:

Crystal structure of human protein tyrosine phosphatase kappa at 1.95a resolution

Structure:

Receptor-type tyrosine-protein phosphatase kappa. Chain: a. Fragment: residues 865-1154. Synonym: human protein tyrosine phosphatase kappa, protein-tyrosine phosphatase kappa, r-ptp-kappa. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.95Å R-factor: 0.201 R-free: 0.218

Authors:

J.E.Debreczeni,E.Ugochukwu,J.Eswaran,A.Barr,S.Das,N.Burgess, O.Gileadi,E.Longman,F.Von Delft,S.Knapp,M.Sundstron,C.Arrowsmith, J.Weigelt,A.Edwards

Key ref:

J.Eswaran et al. (2006). The crystal structure of human receptor protein tyrosine phosphatase kappa phosphatase domain 1. Protein Sci, 15, 1500-1505. PubMed id: 16672235 DOI: 10.1110/ps.062128706

Date:

28-Nov-05 Release date: 02-Jan-07

Protein chain

Q15262  (PTPRK_HUMAN) -  Receptor-type tyrosine-protein phosphatase kappa from Homo sapiens

Seq: 1439 a.a.

Struc: 289 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

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: 10.1110/ps.062128706

Protein Sci 15:1500-1505 (2006)

PubMed id: 16672235

The crystal structure of human receptor protein tyrosine phosphatase kappa phosphatase domain 1.

J.Eswaran, J.E.Debreczeni, E.Longman, A.J.Barr, S.Knapp.

ABSTRACT

The receptor-type protein tyrosine phosphatases (RPTPs) are integral membrane proteins composed of extracellular adhesion molecule-like domains, a single transmembrane domain, and a cytoplasmic domain. The cytoplasmic domain consists of tandem PTP domains, of which the D1 domain is enzymatically active. RPTPkappa is a member of the R2A/IIb subfamily of RPTPs along with RPTPmu, RPTPrho, and RPTPlambda. Here, we have determined the crystal structure of catalytically active, monomeric D1 domain of RPTPkappa at 1.9 A. Structural comparison with other PTP family members indicates an overall classical PTP architecture of twisted mixed beta-sheets flanked by alpha-helices, in which the catalytically important WPD loop is in an unhindered open conformation. Though the residues forming the dimeric interface in the RPTPmu structure are all conserved, they are not involved in the protein-protein interaction in RPTPkappa. The N-terminal beta-strand, formed by betax association with betay, is conserved only in RPTPs but not in cytosolic PTPs, and this feature is conserved in the RPTPkappa structure forming a beta-strand. Analytical ultracentrifugation studies show that the presence of reducing agents and higher ionic strength are necessary to maintain RPTPkappa as a monomer. In this family the crystal structure of catalytically active RPTPmu D1 was solved as a dimer, but the dimerization was proposed to be a consequence of crystallization since the protein was monomeric in solution. In agreement, we show that RPTPkappa is monomeric in solution and crystal structure.

Selected figure(s)

Figure 2.
Figure 2. Three-dimensional structure of RPTP . (Red) -Helices; (green) -strands; (magenta) 3[10]-helices. The helix-turn-helix segment ( 1', 2') and the -strand formed by association of x and y are labeled. The corresponding conserved residues involved in dimerization of RPTPµ are shown in ball-and-stick representation.

The above figure is reprinted by permission from the Protein Society: Protein Sci (2006, 15, 1500-1505) copyright 2006.

Figure was selected by an automated process.