PDBsum entry: 1t3k

Hydrolase

PDB id: 1t3k

Contents

Protein chain

132 a.a. *

Metals

_ZN

* Residue conservation analysis

PDB id:

1t3k

Name:

Hydrolase

Title:

Nmr structure of a cdc25-like dual-specificity tyrosine phosphatase of arabidopsis thaliana

Structure:

Dual-specificity tyrosine phosphatase. Chain: a. Synonym: arath cdc25. Engineered: yes. Mutation: yes

Source:

Arabidopsis thaliana. Thale cress. Organism_taxid: 3702. Gene: cdc25. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

I.Landrieu,M.Da Costa,L.De Veylder,F.Dewitte,K.Vandepoele, S.Hassan,J.M.Wieruszeski,J.D.Faure,D.Inze,G.Lippens

Key ref:

I.Landrieu et al. (2004). A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana. Proc Natl Acad Sci U S A, 101, 13380-13385. PubMed id: 15329414 DOI: 10.1073/pnas.0405248101

Date:

27-Apr-04 Release date: 07-Sep-04

Protein chain

Q8GY31  (CDC25_ARATH) -  Dual specificity phosphatase Cdc25

Seq: 146 a.a.

Struc: 132 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: Protein tyrosine phosphate + H₂O = protein tyrosine + phosphate

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

 Gene Ontology (GO) functional annotation 

• Cellular component: nucleus (2 terms)
• Biological process: cell cycle (5 terms)
• Biochemical function: protein binding (6 terms)

reference

DOI no: 10.1073/pnas.0405248101

Proc Natl Acad Sci U S A 101:13380-13385 (2004)

PubMed id: 15329414

A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana.

I.Landrieu, M.da Costa, L.De Veylder, F.Dewitte, K.Vandepoele, S.Hassan, J.M.Wieruszeski, F.Corellou, J.D.Faure, M.Van Montagu, D.Inzé, G.Lippens.

ABSTRACT

The dual-specificity CDC25 phosphatases are critical positive regulators of cyclin-dependent kinases (CDKs). Even though an antagonistic Arabidopsis thaliana WEE1 kinase has been cloned and tyrosine phosphorylation of its CDKs has been demonstrated, no valid candidate for a CDC25 protein has been reported in higher plants. We identify a CDC25-related protein (Arath;CDC25) of A. thaliana, constituted by a sole catalytic domain. The protein has a tyrosine-phosphatase activity and stimulates the kinase activity of Arabidopsis CDKs. Its tertiary structure was obtained by NMR spectroscopy and confirms that Arath;CDC25 belongs structurally to the classical CDC25 superfamily with a central five-stranded beta-sheet surrounded by helices. A particular feature of the protein, however, is the presence of an additional zinc-binding loop in the C-terminal part. NMR mapping studies revealed the interaction with phosphorylated peptidic models derived from the conserved CDK loop containing the phosphothreonine-14 and phosphotyrosine-15. We conclude that despite sequence divergence, Arath;CDC25 is structurally and functionally an isoform of the CDC25 superfamily, which is conserved in yeast and in plants, including Arabidopsis and rice.

Selected figure(s)

Figure 1.
Fig. 1. Sequence comparison of the Arath;CDC25 protein with CDC25, small CDC25-like tyrosine phosphatases, and the yeast arsenate reductase ACR2. Identical amino acids in all of the sequences are shown in white on a black background. Conserved amino acids are in bold. Secondary structure elements are indicated above the alignment for human CDC25A (PDB ID 1C25 [PDB] ) and below for A. thaliana Arath;CDC25. The catalytic loop is indicated by the HC(X)[5]R motif. CDC25ACDC25A_human, human CDC25A (accession number NP_001780 [GenBank] ); CDC25B_human, human CDC25B (NP_068658 [GenBank] ); CDC25C_human, human CDC25C (NP_073720 [GenBank] ); CDC25_pombe, Sch. pombe CDC25 (NP_013750 [GenBank] ); MIH1_cerevisiae, S. cerevisiae CDC25 (NP_013750 [GenBank] ); YGR203_cerevisiae, S. cerevisiae protein of unknown function (NP_011719 [GenBank] ); ACR2_cerevisiae, S. cerevisiae arsenate reductase (NP_015526 [GenBank] ); IBP1_pombe, Sch. pombe small CDC25-like protein (AL096796 [GenBank] ); Orysa;CDC25;1, O. sativa protein of unknown function (NP_922597 [GenBank] ); Arath;CDC25_Arabidop, this work (NP_568119 [GenBank] ).

Figure 3.
Fig. 3. Ribbon representation in the same orientation of the backbone of a representative conformer of the Arath;CDC25 protein (Left) and the human CDC25A (Right) (PDB entry 1C25 [PDB] , ref. 4). The conserved five-stranded -sheet and 4 helices of the structures have been superposed as described in Results. The catalytic loop is indicated by the HC(X)[5]R motif. The zinc ion is represented as a black sphere.

Figures were selected by an automated process.