1ZPQ

STRUCTURE OF BACTERIOPHAGE LAMBDA CII protein

Summary for 1ZPQ

• Entry DOI: 10.2210/pdb1zpq/pdb
• Descriptor: Regulatory protein CII (2 entities in total)
• Functional Keywords: helix-turn-helix, transcription activation, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, transcription activator
• Biological source: Enterobacteria phage lambda
• Total number of polymer chains: 4
• Total formula weight: 44291.63

Authors

Jain, D.,Kim, Y.,Maxwell, K.L.,Beasley, S.,Gussin, G.N.,Edwards, A.M.,Joachimiak, A.,Darst, S.A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2005-05-17, release date: 2005-08-23, Last modification date: 2024-02-14)

Primary citation

Jain, D.,Kim, Y.,Maxwell, K.L.,Beasley, S.,Zhang, R.,Gussin, G.N.,Edwards, A.M.,Darst, S.A.
Crystal Structure of Bacteriophage lambdacII and Its DNA Complex.
Mol.Cell, 19:259-269, 2005

PubMed 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.

PubMed: 16039594
DOI: 10.1016/j.molcel.2005.06.006

Experimental method

X-RAY DIFFRACTION (2.8 Å)