Cargando…
The Carboxy-Terminal αN Helix of the Archaeal XerA Tyrosine Recombinase Is a Molecular Switch to Control Site-Specific Recombination
Tyrosine recombinases are conserved in the three kingdoms of life. Here we present the first crystal structure of a full-length archaeal tyrosine recombinase, XerA from Pyrococcus abyssi, at 3.0 Å resolution. In the absence of DNA substrate XerA crystallizes as a dimer where each monomer displays a...
Autores principales: | Serre, Marie-Claude, El Arnaout, Toufic, Brooks, Mark A., Durand, Dominique, Lisboa, Johnny, Lazar, Noureddine, Raynal, Bertrand, van Tilbeurgh, Herman, Quevillon-Cheruel, Sophie |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3646895/ https://www.ncbi.nlm.nih.gov/pubmed/23667562 http://dx.doi.org/10.1371/journal.pone.0063010 |
Ejemplares similares
-
Correction: The Carboxy-Terminal αN Helix of the Archaeal XerA Tyrosine Recombinase Is a Molecular Switch to Control Site-Specific Recombination
por: Serre, Marie-Claude, et al.
Publicado: (2014) -
Evidence for a Xer/dif System for Chromosome Resolution in Archaea
por: Cortez, Diego, et al.
Publicado: (2010) -
Archaeal tyrosine recombinases
por: Badel, Catherine, et al.
Publicado: (2021) -
Xer Site Specific Recombination: Double and Single Recombinase Systems
por: Castillo, Fabio, et al.
Publicado: (2017) -
Functional Analysis of the Acinetobacter baumannii XerC and XerD Site-Specific Recombinases: Potential Role in Dissemination of Resistance Genes
por: Lin, David L., et al.
Publicado: (2020)