5LOI

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

5LOI の概要

• エントリーDOI: 10.2210/pdb5loi/pdb
• 分子名称: Rad26 (1 entity in total)
• 機能のキーワード: rad26 (atrip), rad3 (atr), dna-damage response (ddr), kinase signaling, signaling protein
• 由来する生物種: Myceliophthora thermophila ATCC 42464
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 51698.38

構造登録者

Andersen, K.R. (登録日: 2016-08-09, 公開日: 2017-03-29, 最終更新日: 2024-11-13)

主引用文献

Andersen, K.R.
Insights into Rad3 kinase recruitment from the crystal structure of the DNA damage checkpoint protein Rad26.
J. Biol. Chem., 292:8149-8157, 2017

PubMed Abstract: 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 is 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 showed 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.

PubMed: 28314775
DOI: 10.1074/jbc.M117.780189

実験手法

X-RAY DIFFRACTION (3.153 Å)