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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Bibliographic Details
Main Authors: Marie-Claude Serre, Toufic El Arnaout, Mark A Brooks, Dominique Durand, Johnny Lisboa, Noureddine Lazar, Bertrand Raynal, Herman van Tilbeurgh, Sophie Quevillon-Cheruel
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2013-01-01
Series:PLoS ONE
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23667562/?tool=EBI