Structural Basis for Catalytic Activation of a Serine Recombinase

Keenholtz, R.A., Rowland, S.-J., Boocock, M.R., Stark, W.M. and Rice, P.A. (2011) Structural Basis for Catalytic Activation of a Serine Recombinase. Structure, 19(6), pp. 799-809. (doi: 10.1016/j.str.2011.03.017)

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Sin resolvase is a site-specific serine recombinase that is normally controlled by a complex regulatory mechanism. A single mutation, Q115R, allows the enzyme to bypass the entire regulatory apparatus, such that no accessory proteins or DNA sites are required. Here, we present a 1.86 angstrom crystal structure of the Sin Q115R catalytic domain, in a tetrameric arrangement stabilized by an interaction between Arg115 residues on neighboring subunits. The subunits have undergone significant conformational changes from the inactive dimeric state previously reported. The structure provides a new high-resolution view of a serine recombinase active site that is apparently fully assembled, suggesting roles for the conserved active site residues. The structure also suggests how the dimer-tetramer transition is coupled to assembly of the active site. The tetramer is captured in a different rotational substate than that seen in previous hyperactive serine recombinase structures, and unbroken crossover site DNA can be readily modeled into its active sites

Item Type:Articles
Glasgow Author(s) Enlighten ID:Rowland, Dr Sally-Jane and Boocock, Dr Martin and Stark, Professor Marshall
Authors: Keenholtz, R.A., Rowland, S.-J., Boocock, M.R., Stark, W.M., and Rice, P.A.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Structure

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