1BJA

ACTIVATION DOMAIN OF THE PHAGE T4 TRANSCRIPTION FACTOR MOTA

1BJA の概要

• エントリーDOI: 10.2210/pdb1bja/pdb
• 分子名称: TRANSCRIPTION REGULATORY PROTEIN MOTA, SULFATE ION (3 entities in total)
• 機能のキーワード: activation domain, phage t4, middle mode transcription, alpha helical structure, transcription regulation
• 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: 20325.21

構造登録者

Finnin, M.S.,Cicero, M.P.,Davies, C.,Porter, S.J.,White, S.W.,Kreuzer, K.N. (登録日: 1998-06-23, 公開日: 1998-11-04, 最終更新日: 2024-02-07)

主引用文献

Finnin, M.S.,Cicero, M.P.,Davies, C.,Porter, S.J.,White, S.W.,Kreuzer, K.N.
The activation domain of the MotA transcription factor from bacteriophage T4.
EMBO J., 16:1992-2003, 1997

PubMed Abstract: Bacteriophage T4 encodes a transcription factor, MotA, that binds to the -30 region of middle-mode promoters and activates transcription by host RNA polymerase. We have solved the structure of the MotA activation domain to 2.2 A by X-ray crystallography, and have also determined its secondary structure by NMR. An area on the surface of the protein has a distinctive patch that is populated with acidic and hydrophobic residues. Mutations within this patch cause a defective T4 growth phenotype, arguing that the patch is important for MotA function. One of the mutant MotA activation domains was purified and analyzed by NMR, and the spectra clearly show that the domain is properly folded. The mutant full-length protein appears to bind DNA normally but is deficient in transcriptional activation. We conclude that the acidic/hydrophobic surface patch is specifically involved in transcriptional activation, which is reminiscent of eukaryotic acidic activation domains.

PubMed: 9155025
DOI: 10.1093/emboj/16.8.1992

実験手法

X-RAY DIFFRACTION (2.19 Å)