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...
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Autores principales: | Marie-Claude Serre, Toufic El Arnaout, Mark A Brooks, Dominique Durand, Johnny Lisboa, Noureddine Lazar, Bertrand Raynal, Herman van Tilbeurgh, Sophie Quevillon-Cheruel |
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Formato: | article |
Lenguaje: | EN |
Publicado: |
Public Library of Science (PLoS)
2013
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Materias: | |
Acceso en línea: | https://doaj.org/article/873f6b13116a45c58203ea25d418ca3e |
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