2R0Q

Crystal structure of a serine recombinase- DNA regulatory complex

Summary for 2R0Q

• Entry DOI: 10.2210/pdb2r0q/pdb
• Related: 1gdt 1zr4 2gm4 2gm5 2rsl
• Descriptor: 31-MER, Putative transposon Tn552 DNA-invertase bin3, SULFATE ION, ... (4 entities in total)
• Functional Keywords: site-specific recombinase, resolvase, dna-binding protein, protein-dna complex, dna integration, dna invertase, dna recombination, plasmid, transposable element, transposition, recombination-dna complex, recombination/dna
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 8
• Total formula weight: 135553.37

Authors

Rice, P.A.,Mouw, K.W. (deposition date: 2007-08-21, release date: 2008-04-01, Last modification date: 2024-02-21)

Primary citation

Mouw, K.W.,Rowland, S.J.,Gajjar, M.M.,Boocock, M.R.,Stark, W.M.,Rice, P.A.
Architecture of a serine recombinase-DNA regulatory complex.
Mol.Cell, 30:145-155, 2008

PubMed Abstract: An essential feature of many site-specific recombination systems is their ability to regulate the direction and topology of recombination. Resolvases from the serine recombinase family assemble an interwound synaptic complex that harnesses negative supercoiling to drive the forward reaction and promote recombination between properly oriented sites. To better understand the interplay of catalytic and regulatory functions within these synaptic complexes, we have solved the structure of the regulatory site synapse in the Sin resolvase system. It reveals an unexpected synaptic interface between helix-turn-helix DNA-binding domains that is also highlighted in a screen for synapsis mutants. The tetramer defined by this interface provides the foundation for a robust model of the synaptic complex, assembled entirely from available crystal structures, that gives insight into how the catalytic activity of Sin and other serine recombinases may be regulated.

PubMed: 18439894
DOI: 10.1016/j.molcel.2008.02.023

Experimental method

X-RAY DIFFRACTION (3.2 Å)