Ontology highlight
ABSTRACT:
SUBMITTER: Sugahara M
PROVIDER: S-EPMC306600 | biostudies-literature | 2000 Aug
REPOSITORIES: biostudies-literature
Sugahara M M Mikawa T T Kumasaka T T Yamamoto M M Kato R R Fukuyama K K Inoue Y Y Kuramitsu S S
The EMBO journal 20000801 15
The MutM [formamidopyrimidine DNA glycosylase (Fpg)] protein is a trifunctional DNA base excision repair enzyme that removes a wide range of oxidatively damaged bases (N-glycosylase activity) and cleaves both the 3'- and 5'-phosphodiester bonds of the resulting apurinic/apyrimidinic site (AP lyase activity). The crystal structure of MutM from an extreme thermophile, Thermus thermophilus HB8, was determined at 1.9 A resolution with multiwavelength anomalous diffraction phasing using the intrinsic ...[more]