Structural highlights
Function
[RPC2_LAMBD] This protein and protein CIII form a complex that is involved in the initiation of lysogeny. The complex binds at either of the cy regulatory sites preceding the CI repressor protein and integrase coding regions and induces transcription of these genes.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of bacteriophage lambda cII and its DNA complex.,Jain D, Kim Y, Maxwell KL, Beasley S, Zhang R, Gussin GN, Edwards AM, Darst SA Mol Cell. 2005 Jul 22;19(2):259-69. PMID:16039594[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jain D, Kim Y, Maxwell KL, Beasley S, Zhang R, Gussin GN, Edwards AM, Darst SA. Crystal structure of bacteriophage lambda cII and its DNA complex. Mol Cell. 2005 Jul 22;19(2):259-69. PMID:16039594 doi:10.1016/j.molcel.2005.06.006
