Ontology highlight
ABSTRACT:
SUBMITTER: Tsurumura T
PROVIDER: S-EPMC3600452 | biostudies-literature | 2013 Mar
REPOSITORIES: biostudies-literature
Tsurumura Toshiharu T Tsumori Yayoi Y Qiu Hao H Oda Masataka M Sakurai Jun J Nagahama Masahiro M Tsuge Hideaki H
Proceedings of the National Academy of Sciences of the United States of America 20130204 11
Clostridium perfringens iota-toxin (Ia) mono-ADP ribosylates Arg177 of actin, leading to cytoskeletal disorganization and cell death. To fully understand the reaction mechanism of arginine-specific mono-ADP ribosyl transferase, the structure of the toxin-substrate protein complex must be characterized. Recently, we solved the crystal structure of Ia in complex with actin and the nonhydrolyzable NAD(+) analog βTAD (thiazole-4-carboxamide adenine dinucleotide); however, the structures of the NAD(+ ...[more]