1DRG

CRYSTAL STRUCTURE OF TRIMERIC CRE RECOMBINASE-LOX COMPLEX

Summary for 1DRG

• Entry DOI: 10.2210/pdb1drg/pdb
• Related: 1CRX 2CRX 3CRX 4CRX 5CRX
• Descriptor: 5'-D(*TP*AP*TP*AP*AP*CP*TP*TP*CP*GP*TP*AP*TP*AP*GP*C)-3', 5'-D(*AP*TP*AP*TP*GP*CP*TP*AP*TP*AP*CP*GP*AP*AP*GP*TP*TP*AP*T)-3', CRE RECOMBINASE, ... (4 entities in total)
• Functional Keywords: site-specific recombinase, recombination, protein-dna complex, trimeric, three- way junction, branched dna, hydrolase, ligase-dna complex, ligase/dna
• Biological source: Enterobacteria phage P1
• Total number of polymer chains: 3
• Total formula weight: 47189.78

Authors

Woods, K.C.,Baldwin, E.P. (deposition date: 2000-01-06, release date: 2001-10-19, Last modification date: 2024-02-07)

Primary citation

Woods, K.C.,Martin, S.S.,Chu, V.C.,Baldwin, E.P.
Quasi-equivalence in site-specific recombinase structure and function: crystal structure and activity of trimeric Cre recombinase bound to a three-way Lox DNA junction
J.Mol.Biol., 313:49-69, 2001

PubMed Abstract: The crystal structure of a novel Cre-Lox synapse was solved using phases from multiple isomorphous replacement and anomalous scattering, and refined to 2.05 A resolution. In this complex, a symmetric protein trimer is bound to a Y-shaped three-way DNA junction, a marked departure from the pseudo-4-fold symmetrical tetramer associated with Cre-mediated LoxP recombination. The three-way DNA junction was accommodated by a simple kink without significant distortion of the adjoining DNA duplexes. Although the mean angle between DNA arms in the Y and X structures was similar, adjacent Cre trimer subunits rotated 29 degrees relative to those in the tetramers. This rotation was accommodated at the protein-protein and DNA-DNA interfaces by interactions that are "quasi-equivalent" to those in the tetramer, analogous to packing differences of chemically identical viral subunits at non-equivalent positions in icosahedral capsids. This structural quasi-equivalence extends to function as Cre can bind to, cleave and perform strand transfer with a three-way Lox substrate. The structure explains the dual recognition of three and four-way junctions by site-specific recombinases as being due to shared structural features between the differently branched substrates and plasticity of the protein-protein interfaces. To our knowledge, this is the first direct demonstration of quasi-equivalence in both the assembly and function of an oligomeric enzyme.

PubMed: 11601846
DOI: 10.1006/jmbi.2001.5012

Experimental method

X-RAY DIFFRACTION (2.55 Å)