Cargando…
Solution structure and DNA-binding properties of the phosphoesterase domain of DNA ligase D
The phosphoesterase (PE) domain of the bacterial DNA repair enzyme LigD possesses distinctive manganese-dependent 3′-phosphomonoesterase and 3′-phosphodiesterase activities. PE exemplifies a new family of DNA end-healing enzymes found in all phylogenetic domains. Here, we determined the structure of...
Autores principales: | Natarajan, Aswin, Dutta, Kaushik, Temel, Deniz B., Nair, Pravin A., Shuman, Stewart, Ghose, Ranajeet |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3300020/ https://www.ncbi.nlm.nih.gov/pubmed/22084199 http://dx.doi.org/10.1093/nar/gkr950 |
Ejemplares similares
-
Structures and activities of archaeal members of the LigD 3′-phosphoesterase DNA repair enzyme superfamily
por: Smith, Paul, et al.
Publicado: (2011) -
Structural insights to the metal specificity of an archaeal member of the LigD 3′-phosphoesterase DNA repair enzyme family
por: Das, Ushati, et al.
Publicado: (2012) -
Characterization of Agrobacterium tumefaciens DNA ligases C and D
por: Zhu, Hui, et al.
Publicado: (2007) -
Kinetic mechanism and fidelity of nick sealing by Escherichia coli NAD(+)-dependent DNA ligase (LigA)
por: Chauleau, Mathieu, et al.
Publicado: (2016) -
Structural basis for the GTP specificity of the RNA kinase domain of fungal tRNA ligase
por: Remus, Barbara S., et al.
Publicado: (2017)