2CRX
STRUCTURE OF THE HOLLIDAY JUNCTION INTERMEDIATE IN CRE-LOXP SITE-SPECIFIC RECOMBINATION
Summary for 2CRX
| Entry DOI | 10.2210/pdb2crx/pdb |
| Descriptor | DNA 35-MER, PROTEIN (CRE RECOMBINASE) (3 entities in total) |
| Functional Keywords | cre recombinase, holliday junction, recombination, recombinase-dna complex, hydrolase, ligase-dna complex, ligase/dna |
| Biological source | Enterobacteria phage P1 |
| Total number of polymer chains | 4 |
| Total formula weight | 98710.26 |
| Authors | Gopaul, D.N.,Guo, F.,Vanduyne, G.D. (deposition date: 1998-06-19, release date: 1999-12-14, Last modification date: 2023-08-23) |
| Primary citation | Gopaul, D.N.,Guo, F.,Van Duyne, G.D. Structure of the Holliday junction intermediate in Cre-loxP site-specific recombination. EMBO J., 17:4175-4187, 1998 Cited by PubMed Abstract: We have determined the X-ray crystal structures of two DNA Holliday junctions (HJs) bound by Cre recombinase. The HJ is a four-way branched structure that occurs as an intermediate in genetic recombination pathways, including site-specific recombination by the lambda-integrase family. Cre recombinase is an integrase family member that recombines 34 bp loxP sites in the absence of accessory proteins or auxiliary DNA sequences. The 2.7 A structure of Cre recombinase bound to an immobile HJ and the 2.5 A structure of Cre recombinase bound to a symmetric, nicked HJ reveal a nearly planar, twofold-symmetric DNA intermediate that shares features with both the stacked-X and the square conformations of the HJ that exist in the unbound state. The structures support a protein-mediated crossover isomerization of the junction that acts as the switch responsible for activation and deactivation of recombinase active sites. In this model, a subtle isomerization of the Cre recombinase-HJ quaternary structure dictates which strands are cleaved during resolution of the junction via a mechanism that involves neither branch migration nor helical restacking. PubMed: 9670032DOI: 10.1093/emboj/17.14.4175 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
Download full validation report
