Protein kinase Spk1: Difference between revisions

Latest revision as of 11:57, 3 February 2022

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).

Drag the structure with the mouse to rotate

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

Updated on 03-February-2022

ReferencesReferences

↑ 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
↑ 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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Michal Harel, Alexander Berchansky, Joel L. Sussman

[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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[2]

@@ Line 1: / Line 1: @@
-<StructureSection load='2a0t' size='340' side='right' caption='Structure of yeast Rad53 FHA1 domain (grey) complex with phosphothreonine peptide (green) (PDB code [[2a0t]]).' 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 ==
-'''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 ==
-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>
@@ Line 16: / Line 16: @@
 {{#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]], [[2jqi]] – yRad53 FHA1 domain + phosphothreonine peptide <br />
+**[[1g6g]], [[2a0t]] – yRad53 + PTO peptide <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 />
 **[[4pds]] – yRad53 kinase and SCD2 domain (mutant) + AMPPNP<br />
+*Rad53 residues 1-466
+**[[5xzw]] – yRad53  <br />
+**[[5xzv]] – yRad53 + AMPPNP<br />
 }}