Cargando…
Structural basis for the nuclease activity of a bacteriophage large terminase
The DNA-packaging motor in tailed bacteriophages requires nuclease activity to ensure that the genome is packaged correctly. This nuclease activity is tightly regulated as the enzyme is inactive for the duration of DNA translocation. Here, we report the X-ray structure of the large terminase nucleas...
Autores principales: | Smits, Callum, Chechik, Maria, Kovalevskiy, Oleg V, Shevtsov, Mikhail B, Foster, Andrew W, Alonso, Juan C, Antson, Alfred A |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2009
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2685612/ https://www.ncbi.nlm.nih.gov/pubmed/19444313 http://dx.doi.org/10.1038/embor.2009.53 |
Ejemplares similares
-
The putative small terminase from the thermophilic dsDNA bacteriophage G20C is a nine-subunit oligomer
por: Loredo-Varela, Juan, et al.
Publicado: (2013) -
Structure of HK97 small terminase:DNA complex unveils a novel DNA binding mechanism by a circular protein
por: Chechik, Maria, et al.
Publicado: (2023) -
Structure of the large terminase from a hyperthermophilic virus reveals a unique mechanism for oligomerization and ATP hydrolysis
por: Xu, Rui-Gang, et al.
Publicado: (2017) -
Recombinant portal protein from Staphylococcus epidermidis bacteriophage CNPH82 is a 13-subunit oligomer
por: Luan, Weisha, et al.
Publicado: (2012) -
Viral genome packaging terminase cleaves DNA using the canonical RuvC-like two-metal catalysis mechanism
por: Xu, Rui-Gang, et al.
Publicado: (2017)