Ontology highlight
ABSTRACT:
SUBMITTER: Richards JD
PROVIDER: S-EPMC3434800 | biostudies-literature | 2008 Feb
REPOSITORIES: biostudies-literature
Richards Jodi D JD Johnson Kenneth A KA Liu Huanting H McRobbie Anne-Marie AM McMahon Stephen S Oke Muse M Carter Lester L Naismith James H JH White Malcolm F MF
The Journal of biological chemistry 20071204 8
Hel308 is a superfamily 2 helicase conserved in eukaryotes and archaea. It is thought to function in the early stages of recombination following replication fork arrest and has a specificity for removal of the lagging strand in model replication forks. A homologous helicase constitutes the N-terminal domain of human DNA polymerase Q. The Drosophila homologue mus301 is implicated in double strand break repair and meiotic recombination. We have solved the high resolution crystal structure of Hel30 ...[more]