1zpq

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spinqualitylabelsall models 1zpq, resolution 2.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURE OF BACTERIOPHAGE LAMBDA CII protein

Overview

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.

About this Structure

1ZPQ is a Single protein structure of sequence from Enterobacteria phage lambda. Full crystallographic information is available from OCA.

Reference

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

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