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PDBsum entry 2ouc

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protein Protein-protein interface(s) links
Hydrolase PDB id
2ouc
Jmol
Contents
Protein chains
132 a.a. *
Waters ×115
* Residue conservation analysis
PDB id:
2ouc
Name: Hydrolase
Title: Crystal structure of the map kinase binding domain of mkp5
Structure: Dual specificity protein phosphatase 10. Chain: a, b. Fragment: rhodanese domain (residues 148-287). Synonym: mitogen-activated protein kinase phosphatase 5, map kinase phosphatase 5, mkp-5. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: mkp5. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.20Å     R-factor:   0.232     R-free:   0.289
Authors: X.Tao,L.Tong
Key ref:
X.Tao and L.Tong (2007). Crystal structure of the MAP kinase binding domain and the catalytic domain of human MKP5. Protein Sci, 16, 880-886. PubMed id: 17400920 DOI: 10.1110/ps.062712807
Date:
10-Feb-07     Release date:   07-Aug-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9Y6W6  (DUS10_HUMAN) -  Dual specificity protein phosphatase 10
Seq:
Struc:
482 a.a.
132 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 1: 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 2: 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

 

 
    reference    
 
 
DOI no: 10.1110/ps.062712807 Protein Sci 16:880-886 (2007)
PubMed id: 17400920  
 
 
Crystal structure of the MAP kinase binding domain and the catalytic domain of human MKP5.
X.Tao, L.Tong.
 
  ABSTRACT  
 
MAP kinase phosphatases (MKPs) have crucial roles in regulating the signaling activity of MAP kinases and are potential targets for drug discovery against human diseases. These enzymes contain a catalytic domain (CD) as well as a binding domain (BD) that help recognize the target MAP kinase. We report here the crystal structures at up to 2.2 A resolution of the BD and CD of human MKP5 and compare them to the known structures from other MKPs. Dramatic structural differences are observed between the BD of MKP5 and that of MKP3 determined previously by NMR. In particular, the cluster of positively charged residues that is important for MAP kinase binding is located in completely different positions in the two structures, with a distance of 25 A between them. Moreover, this cluster is alpha-helical in MKP5, while it forms a loop followed by a beta-strand in MKP3. These large structural differences could be associated with the distinct substrate preferences of these phosphatases, but further studies are needed to confirm this. The CD of MKP5 is observed in an active conformation, and two loops in the active site have backbone shifts of up to 5 A relative to the inactive CDs from other MKPs.
 
  Selected figure(s)  
 
Figure 2.
Figure 2. Structure of the MAP kinase binding domain of MKP5. (A) Schematic representation of the structure of the binding domain
Figure 5.
Figure 5. Structural comparison between the catalytic domains of MKP5
 
  The above figures are reprinted by permission from the Protein Society: Protein Sci (2007, 16, 880-886) copyright 2007.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18855677 A.Bakan, J.S.Lazo, P.Wipf, K.M.Brummond, and I.Bahar (2008).
Toward a molecular understanding of the interaction of dual specificity phosphatases with substrates: insights from structure-based modeling and high throughput screening.
  Curr Med Chem, 15, 2536-2544.  
18298792 R.Pulido, and R.Hooft van Huijsduijnen (2008).
Protein tyrosine phosphatases: dual-specificity phosphatases in health and disease.
  FEBS J, 275, 848-866.  
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