PDBsum entry 2esb

Hydrolase

PDB id: 2esb

Contents

Protein chain

162 a.a. *

Ligands

ACT

EPE

Waters ×169

* Residue conservation analysis

PDB id:

2esb

Name:

Hydrolase

Title:

Crystal structure of human dusp18

Structure:

Dual specificity protein phosphatase 18. Chain: a. Synonym: dual specific phosphatase 18, low molecular weight dual specificity phosphatase 20. Engineered: yes

Source:

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

Resolution:

2.00Å R-factor: 0.159 R-free: 0.189

Authors:

S.J.Kim,S.E.Ryu,D.G.Jeong,Y.H.Cho,T.S.Yoon,J.H.Kim

Key ref:

D.G.Jeong et al. (2006). Structure of human DSP18, a member of the dual-specificity protein tyrosine phosphatase family. Acta Crystallogr D Biol Crystallogr, 62, 582-588. PubMed id: 16699184 DOI: 10.1107/S0907444906010109

Date:

25-Oct-05 Release date: 06-Jun-06

Protein chain

Q8NEJ0  (DUS18_HUMAN) -  Dual specificity protein phosphatase 18 from Homo sapiens

Seq: 188 a.a.

Struc: 162 a.a.

Enzyme reactions

• Enzyme class 2: E.C.3.1.3.16 - protein-serine/threonine phosphatase.
• Reaction:
  1. O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphate
  2. O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] + phosphate
• Enzyme class 3: E.C.3.1.3.48 - protein-tyrosine-phosphatase.
• Reaction: O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] + phosphate

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

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

reference

DOI no: 10.1107/S0907444906010109

Acta Crystallogr D Biol Crystallogr 62:582-588 (2006)

PubMed id: 16699184

Structure of human DSP18, a member of the dual-specificity protein tyrosine phosphatase family.

D.G.Jeong, Y.H.Cho, T.S.Yoon, J.H.Kim, J.H.Son, S.E.Ryu, S.J.Kim.

ABSTRACT

The human dual-specificity protein phosphatase 18 (DSP18) gene and its protein product have recently been characterized. Like most DSPs, DSP18 displays dephosphorylating activity towards both phosphotyrosine and phosphothreonine residues. However, DSP18 is distinct from other known DSPs in terms of the existence of approximately 30 residues at the C-terminus of the catalytic domain and an unusual optimum activity profile at 328 K. The crystal structure of human DSP18 has been determined at 2.0 A resolution. The catalytic domain of DSP18 adopts a fold similar to that known for other DSP structures. Although good alignments are found with other DSPs, substantial differences are also found in the regions surrounding the active site, suggesting that DSP18 constitutes a unique structure with a distinct substrate specificity. Furthermore, the residues at the C-terminus fold into two antiparallel beta-strands and participate in extensive interactions with the catalytic domain, explaining the thermostability of DSP18.

Selected figure(s)

Figure 3.
Figure 3 Active site. (a) The difference electron-density map for DSP18 was generated with the final model, omitting the bound HEPES. The stereo map contoured at the 3.0 level was presented as superposed with the refined model. The hydrogen-bonding interactions around the active site are represented by dashed lines. (b) Electrostatic potential surfaces of DSP18 and VHR (PDB code [183]1vhr ) are presented. Positive and negative potentials are coloured blue and red, respectively. Residues near the active site are labelled.

Figure 4.
Figure 4 CT motif. (a) The hydrophobic interactions between the catalytic domain and the CT motif. The side chains of residues involved in the hydrophobic interactions are represented and labelled. Residues in the catalytic domain are coloured grey, whereas those in the CT motif are coloured red. (b) Difference F[o] - F[c] electron-density map around the CT motif omitted for map calculation drawn in stereo with the refined model. The map was contoured at a level of 3.0 . Residues with atoms that participate in crystal contacts with neighbours are coloured cyan.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2006, 62, 582-588) copyright 2006.

Figures were selected by an automated process.