ISSN:
1056-8700
Source:
Annual Reviews Electronic Back Volume Collection 1932-2001ff
Topics:
Biology
,
Physics
Notes:
Abstract 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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1146/annurev.biophys.32.110601.141732
