1ae9
|
STRUCTURE OF THE LAMBDA INTEGRASE CATALYTIC CORE
OverviewOverview
Lambda integrase is archetypic of site-specific recombinases that catalyze intermolecular DNA rearrangements without energetic input. DNA cleavage, strand exchange, and religation steps are linked by a covalent phosphotyrosine intermediate in which Tyr342 is attached to the 3'-phosphate of the DNA cut site. The 1.9 angstrom crystal structure of the integrase catalytic domain reveals a protein fold that is conserved in organisms ranging from archaebacteria to yeast and that suggests a model for interaction with target DNA. The attacking Tyr342 nucleophile is located on a flexible loop about 20 angstroms from a basic groove that contains all the other catalytically essential residues. This bipartite active site can account for several apparently paradoxical features of integrase family recombinases, including the capacity for both cis and trans cleavage of DNA.
About this StructureAbout this Structure
1AE9 is a Single protein structure of sequence from Enterobacteria phage lambda. Full crystallographic information is available from OCA.
ReferenceReference
Flexibility in DNA recombination: structure of the lambda integrase catalytic core., Kwon HJ, Tirumalai R, Landy A, Ellenberger T, Science. 1997 Apr 4;276(5309):126-31. PMID:9082984
Page seeded by OCA on Thu Feb 21 11:43:32 2008