3BDN
Crystal Structure of the Lambda Repressor
Summary for 3BDN
| Entry DOI | 10.2210/pdb3bdn/pdb |
| Descriptor | DNA (5'-D(*DAP*DAP*DTP*DAP*DCP*DCP*DAP*DCP*DTP*DGP*DGP*DCP*DGP*DGP*DTP*DGP*DAP*DTP*DAP*DT)-3'), DNA (5'-D(*DTP*DAP*DTP*DAP*DTP*DCP*DAP*DCP*DCP*DGP*DCP*DCP*DAP*DGP*DTP*DGP*DGP*DTP*DAP*DT)-3'), Lambda Repressor (3 entities in total) |
| Functional Keywords | lambda, repressor, allostery, cooperativity, dna binding, transcription-dna complex, transcription/dna |
| Biological source | Enterobacteria phage lambda |
| Total number of polymer chains | 4 |
| Total formula weight | 64364.16 |
| Authors | Stayrook, S.E.,Jaru-Ampornpan, P.,Hochschild, A.,Lewis, M. (deposition date: 2007-11-15, release date: 2008-04-15, Last modification date: 2023-08-30) |
| Primary citation | Stayrook, S.E.,Jaru-Ampornpan, P.,Ni, J.,Hochschild, A.,Lewis, M. Crystal structure of the lambda repressor and a model for pairwise cooperative operator binding Nature, 452:1022-1025, 2008 Cited by PubMed Abstract: Bacteriophage lambda has for many years been a model system for understanding mechanisms of gene regulation. A 'genetic switch' enables the phage to transition from lysogenic growth to lytic development when triggered by specific environmental conditions. The key component of the switch is the cI repressor, which binds to two sets of three operator sites on the lambda chromosome that are separated by about 2,400 base pairs (bp). A hallmark of the lambda system is the pairwise cooperativity of repressor binding. In the absence of detailed structural information, it has been difficult to understand fully how repressor molecules establish the cooperativity complex. Here we present the X-ray crystal structure of the intact lambda cI repressor dimer bound to a DNA operator site. The structure of the repressor, determined by multiple isomorphous replacement methods, reveals an unusual overall architecture that allows it to adopt a conformation that appears to facilitate pairwise cooperative binding to adjacent operator sites. PubMed: 18432246DOI: 10.1038/nature06831 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.909 Å) |
Structure validation
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