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PDBsum entry 2f49

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protein ligands metals Protein-protein interface(s) links
Transferase PDB id
2f49
Jmol
Contents
Protein chains
335 a.a. *
19 a.a. *
Ligands
SCN ×7
Metals
_MG ×2
Waters ×478
* Residue conservation analysis
PDB id:
2f49
Name: Transferase
Title: Crystal structure of fus3 in complex with a ste5 peptide
Structure: Mitogen-activated protein kinase fus3. Chain: a, b. Fragment: fus3. Synonym: map kinase fus3. Engineered: yes. Mutation: yes. Ste5 peptide. Chain: c. Fragment: fus3 binding region of ste5.
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: fus3, dac2. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: this peptide was chemically synthesized but this sequence naturally occurs in the ste5 protein from s.
Biol. unit: Monomer (from PQS)
Resolution:
1.90Å     R-factor:   0.201     R-free:   0.234
Authors: A.Remenyi
Key ref:
A.Breitkreutz and M.Tyers (2006). Cell signaling. A sophisticated scaffold wields a new trick. Science, 311, 789-790. PubMed id: 16469909 DOI: 10.1126/science.1124620
Date:
22-Nov-05     Release date:   28-Mar-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P16892  (FUS3_YEAST) -  Mitogen-activated protein kinase FUS3
Seq:
Struc:
353 a.a.
335 a.a.*
Protein chain
No UniProt id for this chain
Struc: 19 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.2.7.11.24  - Mitogen-activated protein kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a protein = ADP + a phosphoprotein
ATP
+ protein
= ADP
+ phosphoprotein
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     periplasmic space   4 terms 
  Biological process     conjugation   13 terms 
  Biochemical function     nucleotide binding     10 terms  

 

 
    reference    
 
 
DOI no: 10.1126/science.1124620 Science 311:789-790 (2006)
PubMed id: 16469909  
 
 
Cell signaling. A sophisticated scaffold wields a new trick.
A.Breitkreutz, M.Tyers.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
The mating pathway in budding yeast. In response to ligand-induced activation of a pheromone receptor, activated G protein subunits in the membrane recruit and oligomerize Ste5, which in conjunction with the PAK-like kinase Ste20, activates the MAPK module. Once activated, the MAPKs Fus3 and Kss1 phosphorylate a variety of proteins that effect the pheromone response, including the transcription factor Ste12 and the polarization factor and cyclin-dependent kinase inhibitor Far1. Not all signaling components or substrates are shown [see (2) for details]. (Inset) Circle indicates peptide motif from Ste5 that docks specifically into the A site of Fus3. Squares indicate the peptide motifs from Ste5, the MAPK kinase Ste7, and various substrates that dock into the B sites of both Fus3 and Kss1; the star on Far1 indicates that it is a Fus3-specific substrate (9).
 
  The above figure is reprinted by permission from the AAAs: Science (2006, 311, 789-790) copyright 2006.