Ontology highlight
ABSTRACT:
SUBMITTER: Das D
PROVIDER: S-EPMC2839085 | biostudies-literature | 2010 Apr
REPOSITORIES: biostudies-literature
Das Debanu D Moiani Davide D Axelrod Herbert L HL Miller Mitchell D MD McMullan Daniel D Jin Kevin K KK Abdubek Polat P Astakhova Tamara T Burra Prasad P Carlton Dennis D Chiu Hsiu-Ju HJ Clayton Thomas T Deller Marc C MC Duan Lian L Ernst Dustin D Feuerhelm Julie J Grant Joanna C JC Grzechnik Anna A Grzechnik Slawomir K SK Han Gye Won GW Jaroszewski Lukasz L Klock Heath E HE Knuth Mark W MW Kozbial Piotr P Krishna S Sri SS Kumar Abhinav A Marciano David D Morse Andrew T AT Nigoghossian Edward E Okach Linda L Paulsen Jessica J Reyes Ron R Rife Christopher L CL Sefcovic Natasha N Tien Henry J HJ Trame Christine B CB van den Bedem Henry H Weekes Dana D Xu Qingping Q Hodgson Keith O KO Wooley John J Elsliger Marc-André MA Deacon Ashley M AM Godzik Adam A Lesley Scott A SA Tainer John A JA Wilson Ian A IA
Journal of molecular biology 20100201 3
Mre11 nuclease plays a central role in the repair of cytotoxic and mutagenic DNA double-strand breaks. As X-ray structural information has been available only for the Pyrococcus furiosus enzyme (PfMre11), the conserved and variable features of this nuclease across the domains of life have not been experimentally defined. Our crystal structure and biochemical studies demonstrate that TM1635 from Thermotoga maritima, originally annotated as a putative nuclease, is an Mre11 endo/exonuclease (TmMre1 ...[more]