Crystallization and X-ray diffraction analysis of the ternary complex of the C-terminal domain of human REV1 in complex with REV7 bound to a REV3 fragment involved in translesion DNA synthesis.

Sotaro Kikuchi, Kodai Hara, Toshiyuki Shimizu, Mamoru Sato, Hiroshi Hashimoto

Acta crystallographica. Section F, Structural biology and crystallization communications 2012 Aug 01

filter terms:

REV1, REV3 and REV7 are pivotal proteins in translesion DNA synthesis that allows DNA synthesis to continue even in the presence of DNA damage. REV1 and REV3 are error-prone DNA polymerases, while REV7 acts as an adaptor protein that links them together. A ternary complex of the C-terminal domain of human REV1 in complex with REV7 bound to a REV3 fragment has been crystallized. The crystals belonged to space group P3(1)21, with unit-cell parameters a = b = 74.7, c = 124.5 Å.

Citation

Sotaro Kikuchi, Kodai Hara, Toshiyuki Shimizu, Mamoru Sato, Hiroshi Hashimoto. Crystallization and X-ray diffraction analysis of the ternary complex of the C-terminal domain of human REV1 in complex with REV7 bound to a REV3 fragment involved in translesion DNA synthesis. Acta crystallographica. Section F, Structural biology and crystallization communications. 2012 Aug 01;68(Pt 8):962-4