PMID:16039594

Citation	Jain, D, Kim, Y, Maxwell, KL, Beasley, S, Zhang, R, Gussin, GN, Edwards, AM and Darst, SA (2005) Crystal structure of bacteriophage lambda cII and its DNA complex. Mol. Cell 19:259-69
Abstract	The tetrameric cII protein from bacteriophage lambda activates transcription from the phage promoters P(RE), P(I), and P(AQ) by binding to two direct repeats that flank the promoter -35 element. Here, we present the X-ray crystal structure of cII alone (2.8 A resolution) and in complex with its DNA operator from P(RE) (1.7 A resolution). The structures provide a basis for modeling of the activation complex with the RNA polymerase holoenzyme, and point to the key role for the RNA polymerase alpha subunit C-terminal domain (alphaCTD) in cII-dependent activation, which forms a bridge of protein/protein interactions between cII and the RNA polymerase sigma subunit. The model makes specific predictions for protein/protein interactions between cII and alphaCTD, and between alphaCTD and sigma, which are supported by previous genetic studies.
Links	PubMed Online version:10.1016/j.molcel.2005.06.006
Keywords	Bacteriophage lambda/chemistry; Crystallography, X-Ray; DNA, Bacterial/chemistry; DNA-Directed RNA Polymerases/chemistry; Escherichia coli/chemistry; Models, Molecular; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Transcription Factors/chemistry; Viral Proteins
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