PDBsum entry: 1wrm

Hydrolase

PDB id: 1wrm

Contents

Protein chain

156 a.a. *

Ligands

MES

Waters ×80

* Residue conservation analysis

PDB id:

1wrm

Name:

Hydrolase

Title:

Crystal structure of jsp-1

Structure:

Dual specificity phosphatase 22. Chain: a. Fragment: residues 1-163. Synonym: lmw-dsp2, mitogen-activated protein kinase phosphatase x, jnk-stimulating phosphatase 1. Engineered: yes

Source:

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

Biol. unit:

Monomer (from PQS)

Resolution:

1.50Å R-factor: 0.251 R-free: 0.282

Authors:

T.Yokota,A.Kashima,R.Kato,S.Sugio

Key ref:

T.Yokota et al. (2007). Crystal structure of human dual specificity phosphatase, JNK stimulatory phosphatase-1, at 1.5 A resolution. Proteins, 66, 272-278. PubMed id: 17068812 DOI: 10.1002/prot.21152

Date:

22-Oct-04 Release date: 22-Oct-05

Protein chain

Q9NRW4  (DUS22_HUMAN) -  Dual specificity protein phosphatase 22

Seq: 184 a.a.

Struc: 156 a.a.

Enzyme reactions

• Enzyme class 2: E.C.3.1.3.16 - Phosphoprotein phosphatase.
• Reaction: A phosphoprotein + H₂O = a protein + phosphate
• Enzyme class 3: E.C.3.1.3.48 - Protein-tyrosine-phosphatase.
• Reaction: Protein tyrosine phosphate + H₂O = protein tyrosine + 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

 Gene Ontology (GO) functional annotation 

• Biological process: dephosphorylation (2 terms)
• Biochemical function: phosphatase activity (2 terms)

reference

DOI no: 10.1002/prot.21152

Proteins 66:272-278 (2007)

PubMed id: 17068812

Crystal structure of human dual specificity phosphatase, JNK stimulatory phosphatase-1, at 1.5 A resolution.

T.Yokota, Y.Nara, A.Kashima, K.Matsubara, S.Misawa, R.Kato, S.Sugio.

ABSTRACT

Human JNK stimulatory phosphatase-1 (JSP-1) is a novel member of dual specificity phosphatases. A C-terminus truncated JSP-1 was expressed in Escherichia coli and was crystallized using the sitting-drop vapor diffusion method. Thin-plate crystals obtained at 278 K belong to a monoclinic space group, C2, with unit-cell parameters a = 84.0 A, b = 49.3 A, c = 47.3 A, and beta = 119.5 degrees , and diffract up to 1.5 A resolution at 100 K. The structure of JSP-1 has a single compact (alpha/beta) domain, which consists of six alpha-helices and five beta-strands, and shows a conserved structural scaffold in regard to both DSPs and PTPs. A cleft formed by a PTP-loop at the active site is very shallow, and is occupied by one sulfonate compound, MES, at the bottom. In the binary complex structure of JSP-1 with MES, the conformations of three important segments in regard to the catalytic mechanism are not similar to those in PTP1B. JSP-1 has no loop corresponding to the Lys120-loop of PTP1B, and tryptophan residue corresponding to the substrate-stacking in PTP1B is substituted by alanine residue in JSP-1.

Selected figure(s)

Figure 1.
Figure 1. Sequence alignments of JSP-1 and related DSPs. Human JSP-1 (residue 1-184), human JKAP (residue 1-205), mouse JKAP (residue 1-205), and mouse LMW-DSP2 (residue 1-184) are shown. The segments corresponding to the PTP-loop and WPD-loop in PTP1B are shown in dark gray.

Figure 4.
Figure 4. Residues contributing to the MES-stacking. (a) Hydrogen-bond network of JSP-1 with MES. (b) Superposition of JSP-1-MES complex with VHR-p38 peptide complex. Residues and substrate mimic peptide in JSP-1 and VHR are shown in gray and white, respectively.

The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2007, 66, 272-278) copyright 2007.

Figures were selected by the author.