3VU7

Crystal structure of REV1-REV7-REV3 ternary complex

3VU7 の概要

• エントリーDOI: 10.2210/pdb3vu7/pdb
• 分子名称: DNA repair protein REV1, Mitotic spindle assembly checkpoint protein MAD2B, DNA polymerase zeta catalytic subunit (3 entities in total)
• 機能のキーワード: dna polymerase, dna replication, translesion dna synthesis, dna damage tolerance, dna repair, replication
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus (Probable): Q9UBZ9; Nucleus: Q9UI95; Nucleus (Potential): O60673
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 45828.65

構造登録者

Kikuchi, S.,Hara, K.,Shimizu, T.,Sato, M.,Hashimoto, H. (登録日: 2012-06-20, 公開日: 2012-08-08, 最終更新日: 2023-11-08)

主引用文献

Kikuchi, S.,Hara, K.,Shimizu, T.,Sato, M.,Hashimoto, H.
Structural basis of recruitment of DNA polymerase [zeta] by interaction between REV1 and REV7 proteins
J.Biol.Chem., 287:33847-33852, 2012

PubMed Abstract: REV1, REV3, and REV7 are pivotal proteins in translesion DNA synthesis, which allows DNA synthesis even in the presence of DNA damage. REV1 and REV3 are error-prone DNA polymerases and function as inserter and extender polymerases in this process, respectively. REV7 interacts with both REV1 and REV3, acting as an adaptor that functionally links the two, although the structural basis of this collaboration remains unclear. Here, we show the crystal structure of the ternary complex, composed of the C-terminal domain of human REV1, REV7, and a REV3 fragment. The REV1 C-terminal domain adopts a four-helix bundle that interacts with REV7. A linker region between helices 2 and 3, which is conserved among mammals, interacts with the β-sheet of REV7. Remarkably, the REV7-binding interface is distinct from the binding site of DNA polymerase η or κ. Thus, the REV1 C-terminal domain might facilitate polymerase switching by providing a scaffold for both inserter and extender polymerases to bind. Our structure reveals the basis of DNA polymerase ζ (a complex of REV3 and REV7) recruitment to the stalled replication fork and provides insight into the mechanism of polymerase switching.

PubMed: 22859296
DOI: 10.1074/jbc.M112.396838

実験手法

X-RAY DIFFRACTION (2.8 Å)