PDBsum entry 1gwz

Hydrolase

PDB id: 1gwz

Contents

Protein chain

280 a.a. *

* Residue conservation analysis

PDB id:

1gwz

Name:

Hydrolase

Title:

Crystal structure of the catalytic domain of the protein tyrosine phosphatase shp-1

Structure:

Shp-1. Chain: a. Fragment: catalytic domain. Synonym: protein-tyrosine phosphatase. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.50Å R-factor: 0.209 R-free: 0.293

Authors:

J.Yang,X.Liang,T.Niu,W.Meng,Z.Zhao,G.W.Zhou

Key ref:

J.Yang et al. (1998). Crystal structure of the catalytic domain of protein-tyrosine phosphatase SHP-1. J Biol Chem, 273, 28199-28207. PubMed id: 9774441 DOI: 10.1074/jbc.273.43.28199

Date:

22-Aug-98 Release date: 22-Aug-99

Protein chain

P29350  (PTN6_HUMAN) -  Tyrosine-protein phosphatase non-receptor type 6 from Homo sapiens

Seq: 595 a.a.

Struc: 280 a.a.

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: 10.1074/jbc.273.43.28199

J Biol Chem 273:28199-28207 (1998)

PubMed id: 9774441

Crystal structure of the catalytic domain of protein-tyrosine phosphatase SHP-1.

J.Yang, X.Liang, T.Niu, W.Meng, Z.Zhao, G.W.Zhou.

ABSTRACT

The crystal structures of the protein-tyrosine phosphatase SHP-1 catalytic domain and the complex it forms with the substrate analogue tungstate have been determined and refined to crystallographic R values of 0.209 at 2.5 A resolution and 0.207 at 2.8 A resolution, respectively. Despite low sequence similarity, the catalytic domain of SHP-1 shows high similarity in secondary and tertiary structures with other protein-tyrosine phosphatases (PTPs). In contrast to the conformational changes observed in the crystal structures of PTP1B and Yersinia PTP, the WPD loop (Trp419-Pro428) in the catalytic domain of SHP-1 moves away from the substrate binding pocket after binding the tungstate ion. Sequence alignment and structural analysis suggest that the residues in the WPD loop, especially the amino acid following Asp421, are critical for the movement of WPD loop on binding substrates and the specific activity of protein-tyrosine phosphatases. Our mutagenesis and kinetic measurements have supported this hypothesis.

Selected figure(s)

Figure 3.
Fig. 3. Surface electrostatic potentials of the catalytic domains of PTP1B (a), Yersinia PTP (b), PTP (c), PTPµ (d), SHP-2 (e), and SHP-1 (f). Red and blue represent negative and positive electrostatic potentials, respectively. This figure was prepared by GRASP (39).

Figure 4.
Fig. 4. Representation showing the hydrogen bonds formed between the catalytic domain of SHP-1 and the substrate analogue tungstate ion.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (1998, 273, 28199-28207) copyright 1998.

Figures were selected by an automated process.