New insight into site-specific recombination from Flp recombinase-DNA structures.
The lamba integrase, or tyrosine-based family of site-specific recombinases, plays an important role in a variety of biological processes by inserting, excising, and inverting DNA segments. Flp, encoded by the yeast 2-mum plasmid, is the best-characterized eukaryotic member of this family and is responsible for maintaining the copy number of this plasmid. Over the past several years, structural and biochemical studies have shed light on the details of a common catalytic scheme utilized by these enzymes with interesting variations under different biological contexts. The emergence of new Flp structures and solution data provides insights not only into its unique mechanism of active site assembly and activity regulation but also into the specific contributions of certain protein residues to catalysis.
Chen
Yu
Y
Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois 60637, USA. yuchen@midway.uchicago.edu
Rice
Phoebe A
PA
D001665:Binding Sites; D002384:Catalysis; D004247:DNA / Q000737:chemistry* / Q000378:metabolism*; D004254:DNA Nucleotidyltransferases / Q000737:chemistry* / Q000378:metabolism*; D004789:Enzyme Activation; D046911:Macromolecular Substances; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D011487:Protein Conformation; D011995:Recombination, Genetic; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D014443:Tyrosine / Q000737:chemistry* / Q000378:metabolism
D046911:Macromolecular Substances; D014443:Tyrosine; D004247:DNA; D004254:DNA Nucleotidyltransferases; C045119:FLP recombinase