Open AccessCrystallization 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
Author(s) -
Kikuchi Sotaro,
Hara Kodai,
Shimizu Toshiyuki,
Sato Mamoru,
Hashimoto Hiroshi
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112032435
Subject(s) - dna , dna synthesis , ternary complex , dna damage , biology , crystallography , biochemistry , chemistry , enzyme
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 P 3 1 21, with unit‐cell parameters a = b = 74.7, c = 124.5 Å.