1Z1B

Crystal structure of a lambda integrase dimer bound to a COC' core site

Summary for 1Z1B

• Entry DOI: 10.2210/pdb1z1b/pdb
• Related: 1KJK 1P7D 1Z19 1Z1G
• Descriptor: 5'-D(*CP*T*CP*GP*TP*TP*CP*AP*GP*CP*TP*TP*TP*TP*TP*T)-3', 5'-D(*TP*TP*TP*AP*TP*AP*CP*TP*AP*AP*GP*TP*TP*GP*GP*CP*AP*T)-3', 29-MER DNA, ... (6 entities in total)
• Functional Keywords: protein-dna complex, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Enterobacteria phage lambda
• Total number of polymer chains: 7
• Total formula weight: 115571.95

Authors

Biswas, T.,Aihara, H.,Radman-Livaja, M.,Filman, D.,Landy, A.,Ellenberger, T. (deposition date: 2005-03-03, release date: 2005-06-28, Last modification date: 2024-10-30)

Primary citation

Biswas, T.,Aihara, H.,Radman-Livaja, M.,Filman, D.,Landy, A.,Ellenberger, T.
A structural basis for allosteric control of DNA recombination by lambda integrase.
Nature, 435:1059-1066, 2005

PubMed Abstract: 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.

PubMed: 15973401
DOI: 10.1038/nature03657

Experimental method

X-RAY DIFFRACTION (3.8 Å)