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3BDN

Crystal Structure of the Lambda Repressor

Summary for 3BDN
Entry DOI10.2210/pdb3bdn/pdb
DescriptorDNA (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 Keywordslambda, repressor, allostery, cooperativity, dna binding, transcription-dna complex, transcription/dna
Biological sourceEnterobacteria phage lambda
Total number of polymer chains4
Total formula weight64364.16
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 citationStayrook, 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: 18432246
DOI: 10.1038/nature06831
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.909 Å)
Structure validation

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