5J0N

Lambda excision HJ intermediate

Summary for 5J0N

• Entry DOI: 10.2210/pdb5j0n/pdb
• EMDB information: 3400
• Descriptor: attP(-117 to +79), attB(-21) to attP(+117), attB(-19 to +21), ... (8 entities in total)
• Functional Keywords: bacteriophage lambda, excision, site-specific recombination, holliday junction, transferase, hydrolase-dna complex, hydrolase/dna
• Biological source: Enterobacteria phage lambda; More
• Total number of polymer chains: 15
• Total formula weight: 372047.87

Authors

Van Duyne, G.,Grigorieff, N.,Landy, A. (deposition date: 2016-03-28, release date: 2017-02-08, Last modification date: 2024-03-06)

Primary citation

Laxmikanthan, G.,Xu, C.,Brilot, A.F.,Warren, D.,Steele, L.,Seah, N.,Tong, W.,Grigorieff, N.,Landy, A.,Van Duyne, G.D.
Structure of a Holliday junction complex reveals mechanisms governing a highly regulated DNA transaction.
Elife, 5:-, 2016

PubMed Abstract: The molecular machinery responsible for DNA expression, recombination, and compaction has been difficult to visualize as functionally complete entities due to their combinatorial and structural complexity. We report here the structure of the intact functional assembly responsible for regulating and executing a site-specific DNA recombination reaction. The assembly is a 240-bp Holliday junction (HJ) bound specifically by 11 protein subunits. This higher-order complex is a key intermediate in the tightly regulated pathway for the excision of bacteriophage λ viral DNA out of the E. coli host chromosome, an extensively studied paradigmatic model system for the regulated rearrangement of DNA. Our results provide a structural basis for pre-existing data describing the excisive and integrative recombination pathways, and they help explain their regulation.

PubMed: 27223329
DOI: 10.7554/eLife.14313

Experimental method

ELECTRON MICROSCOPY (11 Å)