4KIS

Crystal Structure of a LSR-DNA Complex

Summary for 4KIS

• Entry DOI: 10.2210/pdb4kis/pdb
• Descriptor: Putative integrase [Bacteriophage A118], DNA (26-MER), ZINC ION, ... (6 entities in total)
• Functional Keywords: recombinase domain, zinc-ribbon domain, coiled-coil motif, recombination-dna complex, recombination/dna
• Biological source: Listeria innocua
• Total number of polymer chains: 12
• Total formula weight: 221188.90

Authors

Rutherford, K.,Yuan, P.,Perry, K.,Van Duyne, G.D. (deposition date: 2013-05-02, release date: 2013-07-10, Last modification date: 2024-02-28)

Primary citation

Rutherford, K.,Yuan, P.,Perry, K.,Sharp, R.,Van Duyne, G.D.
Attachment site recognition and regulation of directionality by the serine integrases.
Nucleic Acids Res., 41:8341-8356, 2013

PubMed Abstract: Serine integrases catalyze the integration of bacteriophage DNA into a host genome by site-specific recombination between 'attachment sites' in the phage (attP) and the host (attB). The reaction is highly directional; the reverse excision reaction between the product attL and attR sites does not occur in the absence of a phage-encoded factor, nor does recombination occur between other pairings of attachment sites. A mechanistic understanding of how these enzymes achieve site-selectivity and directionality has been limited by a lack of structural models. Here, we report the structure of the C-terminal domains of a serine integrase bound to an attP DNA half-site. The structure leads directly to models for understanding how the integrase-bound attP and attB sites differ, why these enzymes preferentially form attP × attB synaptic complexes to initiate recombination, and how attL × attR recombination is prevented. In these models, different domain organizations on attP vs. attB half-sites allow attachment-site specific interactions to form between integrase subunits via an unusual protruding coiled-coil motif. These interactions are used to preferentially synapse integrase-bound attP and attB and inhibit synapsis of integrase-bound attL and attR. The results provide a structural framework for understanding, testing and engineering serine integrase function.

PubMed: 23821671
DOI: 10.1093/nar/gkt580

Experimental method

X-RAY DIFFRACTION (3.2 Å)