Cargando…
Structure of the uncomplexed DNA repair enzyme endonuclease VIII indicates significant interdomain flexibility
Escherichia coli endonuclease VIII (Nei) excises oxidized pyrimidines from DNA. It shares significant sequence homology and similar mechanism with Fpg, a bacterial 8-oxoguanine glycosylase. The structure of a covalent Nei–DNA complex has been recently determined, revealing critical amino acid residu...
Autores principales: | Golan, Gali, Zharkov, Dmitry O., Feinberg, Hadar, Fernandes, Andrea S., Zaika, Elena I., Kycia, Jadwiga H., Grollman, Arthur P., Shoham, Gil |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2005
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1199562/ https://www.ncbi.nlm.nih.gov/pubmed/16145054 http://dx.doi.org/10.1093/nar/gki796 |
Ejemplares similares
-
PRC1 uncomplexed
por: Schouten, Sanne, et al.
Publicado: (2022) -
Distinct Mechanisms of Target Search by Endonuclease VIII-like DNA Glycosylases
por: Diatlova, Evgeniia A., et al.
Publicado: (2022) -
Thermodynamics of the DNA Repair Process by Endonuclease VIII
por: Kladova, O. A., et al.
Publicado: (2019) -
Protein O-Fucosyltransferase 1 Undergoes Interdomain Flexibility in Solution
por: Lira-Navarrete, Erandi, et al.
Publicado: (2021) -
Complement Receptors 1 and 2 in Murine Antibody Responses to IgM-Complexed and Uncomplexed Sheep Erythrocytes
por: Rutemark, Christian, et al.
Publicado: (2012)