Ontology highlight
ABSTRACT:
SUBMITTER: Keenholtz RA
PROVIDER: S-EPMC3238390 | biostudies-literature | 2011 Jun
REPOSITORIES: biostudies-literature
Keenholtz Ross A RA Rowland Sally-J SJ Boocock Martin R MR Stark W Marshall WM Rice Phoebe A PA
Structure (London, England : 1993) 20110601 6
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 ...[more]