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PDBsum entry 1wrm

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Hydrolase PDB id
1wrm
Jmol
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    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9NRW4  (DUS22_HUMAN) -  Dual specificity protein phosphatase 22
Seq:
Struc:
184 a.a.
156 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 2: E.C.3.1.3.16  - Protein-serine/threonine phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: [a protein]-serine/threonine phosphate + H2O = [a protein]- serine/threonine + phosphate
[a protein]-serine/threonine phosphate
+ H(2)O
= [a protein]- serine/threonine
+ phosphate
   Enzyme class 3: E.C.3.1.3.48  - Protein-tyrosine-phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Protein tyrosine phosphate + H2O = protein tyrosine + phosphate
Protein tyrosine phosphate
+ H(2)O
= 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 
  GO annot!
  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.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20018849 J.P.Li, Y.N.Fu, Y.R.Chen, and T.H.Tan (2010).
JNK pathway-associated phosphatase dephosphorylates focal adhesion kinase and suppresses cell migration.
  J Biol Chem, 285, 5472-5478.  
19489729 A.Edwards (2009).
Large-scale structural biology of the human proteome.
  Annu Rev Biochem, 78, 541-568.  
17846751 Y.Ogra, T.Kitaguchi, N.Suzuki, and K.T.Suzuki (2008).
In vitro translation with [34S]-labeled methionine, selenomethionine, and telluromethionine.
  Anal Bioanal Chem, 390, 45-51.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.