Cargando…
Structure of a helicase–helicase loader complex reveals insights into the mechanism of bacterial primosome assembly
During the assembly of the bacterial loader-dependent primosome, helicase loader proteins bind to the hexameric helicase ring, deliver it onto the oriC DNA and then dissociate from the complex. Here, to provide a better understanding of this key process, we report the crystal structure of the ~570-k...
Autores principales: | Liu, Bin, Eliason, William K., Steitz, Thomas A. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Pub. Group
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3791466/ https://www.ncbi.nlm.nih.gov/pubmed/24048025 http://dx.doi.org/10.1038/ncomms3495 |
Ejemplares similares
-
Insights into the structure and assembly of the Bacillus subtilis clamp-loader complex and its interaction with the replicative helicase
por: Afonso, José P., et al.
Publicado: (2013) -
Structural Insights of the DciA Helicase Loader in Its Relationship with DNA
por: Cargemel, Claire, et al.
Publicado: (2023) -
The crystal structure of the Thermus aquaticus DnaB helicase monomer
por: Bailey, Scott, et al.
Publicado: (2007) -
The LH–DH module of bacterial replicative helicases is the common binding site for DciA and other helicase loaders
por: Cargemel, Claire, et al.
Publicado: (2023) -
The plant organellar primase-helicase directs template recognition and primosome assembly via its zinc finger domain
por: Peralta-Castro, Antolin, et al.
Publicado: (2023)