PDBsum entry 4jmj

Hydrolase

PDB id: 4jmj

Contents

Protein chain

181 a.a.

Ligands

PO4

Metals

_CL

Waters ×30

PDB id:

4jmj

Name:

Hydrolase

Title:

Structure of dusp11

Structure:

RNA/rnp complex-1-interacting phosphatase. Chain: a. Fragment: unp residues 28-208. Synonym: dual specificity protein phosphatase 11, phosphatase that interacts with RNA/rnp complex 1. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: dusp11, pir1. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.38Å R-factor: 0.180 R-free: 0.219

Authors:

D.G.Jeong,S.J.Kim,S.E.Ryu

Key ref:

D.G.Jeong et al. (2014). The family-wide structure and function of human dual-specificity protein phosphatases. Acta Crystallogr D Biol Crystallogr, 70, 421-435. PubMed id: 24531476 DOI: 10.1107/S1399004713029866

Date:

14-Mar-13 Release date: 26-Feb-14

Protein chain

O75319  (DUS11_HUMAN) -  RNA/RNP complex-1-interacting phosphatase from Homo sapiens

Seq: 377 a.a.

Struc: 181 a.a.*

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

Enzyme reactions

• Enzyme class: E.C.3.1.3.- - ?????

DOI no: 10.1107/S1399004713029866

Acta Crystallogr D Biol Crystallogr 70:421-435 (2014)

PubMed id: 24531476

The family-wide structure and function of human dual-specificity protein phosphatases.

D.G.Jeong, C.H.Wei, B.Ku, T.J.Jeon, P.N.Chien, J.K.Kim, S.Y.Park, H.S.Hwang, S.Y.Ryu, H.Park, D.S.Kim, S.J.Kim, S.E.Ryu.

ABSTRACT

Dual-specificity protein phosphatases (DUSPs), which dephosphorylate both phosphoserine/threonine and phosphotyrosine, play vital roles in immune activation, brain function and cell-growth signalling. A family-wide structural library of human DUSPs was constructed based on experimental structure determination supplemented with homology modelling. The catalytic domain of each individual DUSP has characteristic features in the active site and in surface-charge distribution, indicating substrate-interaction specificity. The active-site loop-to-strand switch occurs in a subtype-specific manner, indicating that the switch process is necessary for characteristic substrate interactions in the corresponding DUSPs. A comprehensive analysis of the activity-inhibition profile and active-site geometry of DUSPs revealed a novel role of the active-pocket structure in the substrate specificity of DUSPs. A structure-based analysis of redox responses indicated that the additional cysteine residues are important for the protection of enzyme activity. The family-wide structures of DUSPs form a basis for the understanding of phosphorylation-mediated signal transduction and the development of therapeutics.