1P7D

Crystal structure of the Lambda Integrase (residues 75-356) bound to DNA

Summary for 1P7D

• Entry DOI: 10.2210/pdb1p7d/pdb
• Descriptor: 5'-D(*CP*AP*AP*TP*GP*CP*CP*AP*AP*CP*TP*TP*T)-3', 26-MER, Integrase (3 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: 6
• Total formula weight: 87800.73

Authors

Aihara, H.,Kwon, H.J.,Nunes-Duby, S.E.,Landy, A.,Ellenberger, T. (deposition date: 2003-05-01, release date: 2003-08-12, Last modification date: 2024-10-30)

Primary citation

Aihara, H.,Kwon, H.J.,Nunes-Duby, S.E.,Landy, A.,Ellenberger, T.
A Conformational Switch Controls the DNA Cleavage Activity of Lambda Integrase
Mol.Cell, 12:187-198, 2003

PubMed Abstract: The bacteriophage lambda integrase protein (lambda Int) belongs to a family of tyrosine recombinases that catalyze DNA rearrangements. We have determined a crystal structure of lambda Int complexed with a cleaved DNA substrate through a covalent phosphotyrosine bond. In comparison to an earlier unliganded structure, we observe a drastic conformational change in DNA-bound lambda Int that brings Tyr342 into the active site for cleavage of the DNA in cis. A flexible linker connects the central and the catalytic domains, allowing the protein to encircle the DNA. Binding specificity is achieved through direct interactions with the DNA and indirect readout of the flexibility of the att site. The conformational switch that activates lambda Int for DNA cleavage exposes the C-terminal 8 residues for interactions with a neighboring Int molecule. The protein interactions mediated by lambda Int's C-terminal tail offer a mechanism for the allosteric control of cleavage activity in higher order lambda Int complexes.

PubMed: 12887904
DOI: 10.1016/S1097-2765(03)00268-5

Experimental method

X-RAY DIFFRACTION (2.95 Å)