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PDBsum entry 3mbk

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protein ligands Protein-protein interface(s) links
Signaling protein PDB id
3mbk
Jmol
Contents
Protein chains
264 a.a. *
Ligands
SO4 ×2
Waters ×585
* Residue conservation analysis
PDB id:
3mbk
Name: Signaling protein
Title: The 1.35 a structure of the phosphatase domain of the suppre cell receptor signalling protein in complex with sulphate
Structure: Ubiquitin-associated and sh3 domain-containing pr chain: a, b. Fragment: phosphatase domain (unp residues 373-636). Synonym: suppressor of t-cell receptor signaling 1, sts-1, interacting protein p70. Engineered: yes
Source: Mus musculus. Mouse. Organism_taxid: 10090. Gene: ubash3b. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.35Å     R-factor:   0.163     R-free:   0.191
Authors: N.Nassar,J.Jakoncic
Key ref: J.Jakoncic et al. (2010). The 1.35 A resolution structure of the phosphatase domain of the suppressor of T-cell receptor signaling protein in complex with sulfate. Acta Crystallogr Sect F Struct Biol Cryst Commun, 66, 643-647. PubMed id: 20516590
Date:
25-Mar-10     Release date:   23-Jun-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q8BGG7  (UBS3B_MOUSE) -  Ubiquitin-associated and SH3 domain-containing protein B
Seq:
Struc:
 
Seq:
Struc:
638 a.a.
264 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: 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
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Acta Crystallogr Sect F Struct Biol Cryst Commun 66:643-647 (2010)
PubMed id: 20516590  
 
 
The 1.35 A resolution structure of the phosphatase domain of the suppressor of T-cell receptor signaling protein in complex with sulfate.
J.Jakoncic, B.Sondgeroth, N.Carpino, N.Nassar.
 
  ABSTRACT  
 
The suppressor of T-cell signaling (Sts) proteins are multidomain proteins that negatively regulate the signaling of membrane-bound receptors, including the T-cell receptor (TCR) and the epidermal growth-factor receptor (EGFR). They contain at their C-terminus a 2H-phosphatase homology (PGM) domain that is responsible for their protein tyrosine phosphatase activity. Here, the crystal structure of the phosphatase domain of Sts-1, Sts-1(PGM), was determined at pH 4.6. The asymmetric unit contains two independent molecules and each active site is occupied by a sulfate ion. Each sulfate is located at the phosphate-binding site and makes similar interactions with the catalytic residues. The structure suggests an explanation for the lower Michaelis-Menten constants at acidic pH.