3PKZ

Structural basis for catalytic activation of a serine recombinase

Summary for 3PKZ

• Entry DOI: 10.2210/pdb3pkz/pdb
• Related: 2R0Q
• Descriptor: Recombinase Sin, SULFATE ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• Functional Keywords: small serine recombinase, resolvase, dna, recombination
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 12
• Total formula weight: 174774.24

Authors

Keenholtz, R.A.,Boocock, M.R.,Rowland, S.J.,Stark, W.M.,Rice, P.A. (deposition date: 2010-11-12, release date: 2011-06-15, Last modification date: 2024-02-21)

Primary citation

Keenholtz, R.A.,Rowland, S.J.,Boocock, M.R.,Stark, W.M.,Rice, P.A.
Structural basis for catalytic activation of a serine recombinase.
Structure, 19:799-809, 2011

PubMed Abstract: 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 Å 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.

PubMed: 21645851
DOI: 10.1016/j.str.2011.03.017

Experimental method

X-RAY DIFFRACTION (1.8 Å)