1ZPQ: Structure Of Bacteriophage Lambda Cii Protein

Citation:
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.
PDB ID: 1ZPQDownload
MMDB ID: 34746
PDB Deposition Date: 2005/5/17
Updated in MMDB: 2006/12
Experimental Method:
x-ray diffraction
Resolution: 2.8  Å
Source Organism:
Similar Structures:
Biological Unit for 1ZPQ: tetrameric; determined by author and by software (PISA)
Molecular Components in 1ZPQ
Label Count Molecule
Proteins (4 molecules)
4
Regulatory Protein CII(Gene symbol: cII)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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