The crystal structure of the Thermus aquaticus DnaB helicase monomer

The ring-shaped hexameric DnaB helicase unwinds duplex DNA at the replication fork of eubacteria. We have solved the crystal structure of the full-length Thermus aquaticus DnaB monomer, or possibly dimer, at 2.9 Å resolution. DnaB is a highly flexible two domain protein. The C-terminal domain exhibi...

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Detalles Bibliográficos
Autores principales: Bailey, Scott, Eliason, William K., Steitz, Thomas A.
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2007
Materias:
Structural Biology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1950529/
https://www.ncbi.nlm.nih.gov/pubmed/17606462
http://dx.doi.org/10.1093/nar/gkm507

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1950529/
https://www.ncbi.nlm.nih.gov/pubmed/17606462
http://dx.doi.org/10.1093/nar/gkm507

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