Article
Mutations of Asp540 and the domain-connecting residues synergistically enhance Pyrococcus furiosus DNA ligase activity.
FEBS letters - 21 Jan 2014
Tanabe Maiko, Ishino Sonoko, Ishino Yoshizumi, Nishida Hirokazu
Abstract excerpt
The structure of Pyrococcus furiosus DNA ligase (PfuLig), which architecturally resembles human DNA ligase I (hLigI), revealed that the C-terminal helix stabilizes the closed conformation through several ionic interactions between two domains (adenylylation domain (AdD) and C-terminal OB-fold domain (OBD)). This helix is oriented differently in DNA-bound hLigI, suggesting that the disruption of its interactions...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
