CryoEM structures of open dimers of gyrase A in complex with DNA illuminate mechanism of strand passage

Gyrase is a unique type IIA topoisomerase that uses ATP hydrolysis to maintain the negatively supercoiled state of bacterial DNA. In order to perform its function, gyrase undergoes a sequence of conformational changes that consist of concerted gate openings, DNA cleavage, and DNA strand passage even...

Descripción completa

Detalles Bibliográficos
Autores principales: Soczek, Katarzyna M, Grant, Tim, Rosenthal, Peter B, Mondragón, Alfonso
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2018
Materias:
Structural Biology and Molecular Biophysics
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6286129/
https://www.ncbi.nlm.nih.gov/pubmed/30457554
http://dx.doi.org/10.7554/eLife.41215

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6286129/
https://www.ncbi.nlm.nih.gov/pubmed/30457554
http://dx.doi.org/10.7554/eLife.41215

Ejemplares similares