5loi

Crystal structure of Myceliophthora thermophila Rad26 (residues 373-841)

spinqualitylabelsall models 5loi, resolution 3.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5loi is a 1 chain structure with sequence from Thermothelomyces thermophilus ATCC 42464. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.153Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G2QDY6_MYCTT Publication Abstract from PubMed Metabolic products and environmental factors constantly damage DNA. To protect against these insults and maintain genome integrity, cells have evolved mechanisms to repair DNA lesions. One such mechanism involves Rad3, a master kinase coordinating the DNA damage response. Rad26 is a functional subunit of the Rad3-Rad26 complex and responsible for bringing the kinase to sites of DNA damage. Here, I present the crystal structure of Rad26 and identify the elements important for recruiting Rad3. The structure suggests that Rad26 is a dimer with a conserved interface in the N-terminal part of the protein. Biochemical data shows that Rad26 uses its C-terminal domain and the flanking kinase-docking motif to bind specific HEAT repeats in Rad3. Analysis of the reconstituted Rad3-Rad26 heterotetrameric complex with electron microscopy enabled me to propose a structural model for its quaternary structure. In conclusion, these results suggest that Rad26 exists as a dimer and provide crucial insight into how Rad3 is recruited and incorporated into the Rad3-Rad26 DNA repair complex. Insights into Rad3 kinase recruitment from the crystal structure of the DNA damage checkpoint protein Rad26.,Andersen KR J Biol Chem. 2017 Mar 17. pii: jbc.M117.780189. doi: 10.1074/jbc.M117.780189. PMID:28314775 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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