Cargando…
Enzyme–adenylate structure of a bacterial ATP-dependent DNA ligase with a minimized DNA-binding surface
DNA ligases are a structurally diverse class of enzymes which share a common catalytic core and seal breaks in the phosphodiester backbone of double-stranded DNA via an adenylated intermediate. Here, the structure and activity of a recombinantly produced ATP-dependent DNA ligase from the bacterium P...
Autores principales: | Williamson, Adele, Rothweiler, Ulli, Schrøder Leiros, Hanna-Kirsti |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4220977/ https://www.ncbi.nlm.nih.gov/pubmed/25372693 http://dx.doi.org/10.1107/S1399004714021099 |
Ejemplares similares
-
DNA binding with a minimal scaffold: structure–function analysis of Lig E DNA ligases
por: Williamson, Adele, et al.
Publicado: (2018) -
Bacteriophage origin of some minimal ATP-dependent DNA ligases: a new structure from Burkholderia pseudomallei with striking similarity to Chlorella virus ligase
por: Pan, Jolyn, et al.
Publicado: (2021) -
Structural intermediates of a DNA–ligase complex illuminate the role of the catalytic metal ion and mechanism of phosphodiester bond formation
por: Williamson, Adele, et al.
Publicado: (2019) -
Structural insight into DNA joining: from conserved mechanisms to diverse scaffolds
por: Williamson, Adele, et al.
Publicado: (2020) -
ATP-dependent DNA ligases
por: Martin, Ina V, et al.
Publicado: (2002)