1TKV

Solution Structure of T4 AsiA Dimer

「1KA3」から置き換えられました

1TKV の概要

• エントリーDOI: 10.2210/pdb1tkv/pdb
• 分子名称: 10 kDa anti-sigma factor (1 entity in total)
• 機能のキーワード: anti-sigma, homodimer, transcription
• 由来する生物種: Enterobacteria phage T4
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21208.02

構造登録者

Lambert, L.J.,Schirf, V.,Demeler, B.,Cadene, M.,Werner, M.H. (登録日: 2004-06-09, 公開日: 2004-06-22, 最終更新日: 2024-05-22)

主引用文献

Lambert, L.J.,Schirf, V.,Demeler, B.,Cadene, M.,Werner, M.H.
Flipping a genetic switch by subunit exchange
Embo J., 20:7149-7159, 2001

PubMed Abstract: The 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.

PubMed: 11742991
DOI: 10.1093/emboj/20.24.7149

実験手法

SOLUTION NMR