1z1b
|
Crystal structure of a lambda integrase dimer bound to a COC' core site
OverviewOverview
Site-specific DNA recombination is important for basic cellular functions, including viral integration, control of gene expression, production of, genetic diversity and segregation of newly replicated chromosomes, and is, used by bacteriophage lambda to integrate or excise its genome into and, out of the host chromosome. lambda recombination is carried out by the, bacteriophage-encoded integrase protein (lambda-int) together with, accessory DNA sites and associated bending proteins that allow regulation, in response to cell physiology. Here we report the crystal structures of, lambda-int in higher-order complexes with substrates and regulatory DNAs, representing different intermediates along the reaction pathway. The, structures show how the simultaneous binding of two separate domains of, lambda-int to DNA facilitates synapsis and can specify the order of DNA, strand cleavage and exchange. An intertwined layer of amino-terminal, domains bound to accessory (arm) DNAs shapes the recombination complex in, a way that suggests how arm binding shifts the reaction equilibrium in, favour of recombinant products.
About this StructureAbout this Structure
1Z1B is a Single protein structure of sequence from Enterobacteria phage lambda. Full crystallographic information is available from OCA.
ReferenceReference
A structural basis for allosteric control of DNA recombination by lambda integrase., Biswas T, Aihara H, Radman-Livaja M, Filman D, Landy A, Ellenberger T, Nature. 2005 Jun 23;435(7045):1059-66. PMID:15973401
Page seeded by OCA on Wed Nov 21 07:11:18 2007