1tkv
Solution Structure of T4 AsiA Dimer
Structural highlights
FunctionASIA_BPT4 Transcriptional inhibitor. Inhibits sigma 70-directed transcription by weakening its interaction with the core of the host's RNA polymerase. This allows Gp55 to successfully compete for the core enzyme. Plays an important role during the prereplicative period of phage T4 development.[1] [2] 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 PubMedThe bacteriophage T4 AsiA protein is a multifunctional protein that simultaneously acts as both a repressor and activator of gene expression during the phage life cycle. These dual roles with opposing transcriptional consequences are achieved by modification of the host RNA polymerase in which AsiA binds to conserved region 4 (SR4) of sigma(70), altering the pathway of promoter selection by the holoenzyme. The mechanism by which AsiA flips this genetic switch has now been revealed, in part, from the three-dimensional structure of AsiA and the elucidation of its interaction with SR4. The structure of AsiA is that of a novel homodimer in which each monomer is constructed as a seven-helix bundle arranged in four overlapping helix-loop-helix elements. Identification of the protein interfaces for both the AsiA homodimer and the AsiA-sigma(70) complex reveals that these interfaces are coincident. Thus, the AsiA interaction with sigma(70) necessitates that the AsiA homodimer dissociate to form an AsiA-SR4 heterodimer, exchanging one protein subunit for another to alter promoter choice by RNA polymerase. Flipping a genetic switch by subunit exchange.,Lambert LJ, Schirf V, Demeler B, Cadene M, Werner MH EMBO J. 2001 Dec 17;20(24):7149-59. PMID:11742991[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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