Protein kinase Spk1: Difference between revisions

Michal Harel (talk | contribs)
No edit summary
Michal Harel (talk | contribs)
No edit summary
 
(9 intermediate revisions by 3 users not shown)
Line 1: Line 1:
<StructureSection load='1k3n' size='340' side='right' caption='Structure of yeast Rad53 FHA1 domain (grey) complex with phosphothreonine peptide (green) (PDB code [[1k3n]]).' scene=''>
<StructureSection load='' size='350' side='right' caption='Structure of yeast Rad53 FHA1 domain (cyan) complex with phosphothreonine peptide (green) (PDB code [[1k3n]]).' scene='59/590826/Cv/1'>




== Function ==
== Function ==


'''Protein kinase Spk1 (Rad53)''' is a yeast serine/threonine protein kinase which phosphorylates proteins on serene, threonine and tyrosine<ref>PMID:1899289</ref>.  Rad53 controls S-phase checkpoint and G1 and G2 DNA damage checkpoints. Rad53 phosphorylates proteins at serine, threonine and tyrosine residues.
'''Protein kinase Spk1 (Rad53)''' is a yeast serine/threonine protein kinase which phosphorylates proteins on serine, threonine and tyrosine<ref>PMID:1899289</ref>.  Rad53 controls S-phase checkpoint and G1 and G2 DNA damage checkpoints.  


== Structural highlights ==
== Structural highlights ==


Rad53 contains phosphothreonine recognition domains: '''FHA1''' at the N-terminal (residues 1-164) which selects for Asp at position +3 relative to phosphothreonine and '''FHA2''' at the C-terminal (residues 573-730) which selects for Ile at position +3 relative to phosphothreonine. Two '''SCD''' - SQ/TQ-rich cluster domains – are flanking the '''kinase''' domain. SCD domain is associated with DNA-damage-response proteins. The yeast FHA1 domain interacts with peptide containing phosphothreonine<ref>PMID:11106755</ref>.
Rad53 contains phosphothreonine (PTO) recognition domains: '''FHA1''' at the N-terminal (residues 1-164) which selects for Asp at position +3 relative to PTO and '''FHA2''' at the C-terminal (residues 573-730) which selects for Ile at position +3 relative to PTO. Two '''SCD''' - SQ/TQ-rich cluster domains – are flanking the '''kinase''' domain. SCD domain is associated with DNA-damage-response proteins. The <scene name='59/590826/Cv/4'>yeast FHA1 domain interacts with peptide containing PTOXXD sequence</scene><ref>PMID:11846567</ref>.
</StructureSection>
</StructureSection>


Line 16: Line 16:
{{#tree:id=OrganizedByTopic|openlevels=0|
{{#tree:id=OrganizedByTopic|openlevels=0|


*Rad53 FHA1 domain
*Rad53 FHA1 domain 1-164


**[[1k3j]] – yRad53 FHA1 domain – yeast - NMR<br />
**[[1k3j]] – yRad53 – yeast - NMR<br />
**[[1g3g]], [[1j4o]] – yRad53 FHA1 domain (mutant) - NMR<br />
**[[1g3g]], [[1j4o]] – yRad53 (mutant) - NMR<br />
**[[1j4p]], [[1j4q]], [[1k3n]], [[1k3q]] – yRad53 FHA1 domain + Rad9 peptide - NMR<br />
**[[1j4p]], [[1j4q]], [[1k3n]], [[1k3q]] – yRad53 + Rad9 peptide - NMR<br />
**[[1g6g]], [[2a0t]] – yRad53 FHA1 domain + phosphothreonine peptide <br />
**[[1g6g]], [[2a0t]] – yRad53 + PTO peptide <br />
**[[2jqi]] – yRad53 FHA1 domain + phosphothreonine peptide - NMR<br />
**[[2jqi]] – yRad53 + PTO peptide - NMR<br />
**[[5t2f]] - yRad53/DBF4 BRCT domain<br />
**[[5t2s]] - yRad53/DBF4 BRCT domain + phosphopeptide<br />


*Rad53 FHA2 domain
*Rad53 FHA2 domain 573-730


**[[1qu5]], [[1dmz]], [[1fhq]] – yRad53 FHA2 domain – yeast - NMR<br />
**[[1qu5]], [[1dmz]], [[1fhq]] – yRad53 – yeast - NMR<br />
**[[1fhr]], [[1j4k]], [[1j4l]], [[1k2m]], [[1k2n]] – yRad53 FHA2 domain + Rad9 peptide - NMR<br />
**[[1fhr]], [[1j4k]], [[1j4l]], [[1k2m]], [[1k2n]] – yRad53 + Rad9 peptide - NMR<br />


*Rad53 kinase and SCD2 domains
*Rad53 kinase and SCD2 domains residues 170-512


**[[4pdp]] – yRad53 kinase and SCD2 domain (mutant)<br />
**[[4pdp]] – yRad53 kinase and SCD2 domain (mutant)<br />
**[[4pds]] – yRad53 kinase and SCD2 domain (mutant) + AMPPNP<br />
**[[4pds]] – yRad53 kinase and SCD2 domain (mutant) + AMPPNP<br />
*Rad53 residues 1-466
**[[5xzw]] – yRad53  <br />
**[[5xzv]] – yRad53 + AMPPNP<br />
}}
}}


Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman