Function

Protein kinase Spk1 (Rad53) is a yeast serine/threonine protein kinase which phosphorylates proteins on serine, threonine and tyrosine[1]. Rad53 controls S-phase checkpoint and G1 and G2 DNA damage checkpoints.

Structural highlights

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 [2].

Structure of yeast Rad53 FHA1 domain (cyan) complex with phosphothreonine peptide (green) (PDB code 1k3n).

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3D structures of protein kinase Spk13D structures of protein kinase Spk1

Updated on 03-February-2022

ReferencesReferences

  1. Stern DF, Zheng P, Beidler DR, Zerillo C. Spk1, a new kinase from Saccharomyces cerevisiae, phosphorylates proteins on serine, threonine, and tyrosine. Mol Cell Biol. 1991 Feb;11(2):987-1001. PMID:1899289
  2. Yuan C, Yongkiettrakul S, Byeon IJ, Zhou S, Tsai MD. Solution structures of two FHA1-phosphothreonine peptide complexes provide insight into the structural basis of the ligand specificity of FHA1 from yeast Rad53. J Mol Biol. 2001 Nov 30;314(3):563-75. PMID:11846567 doi:10.1006/jmbi.2001.5140

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