1ENW

ELONGATION FACTOR TFIIS DOMAIN II

1ENW の概要

• エントリーDOI: 10.2210/pdb1enw/pdb
• 分子名称: TRANSCRIPTION ELONGATION FACTOR S-II (1 entity in total)
• 機能のキーワード: helix-bundle, transcription
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12732.34

構造登録者

Morin, P.E.,Awrey, D.E.,Edwards, A.M.,Arrowsmith, C.H. (登録日: 2000-03-21, 公開日: 2000-04-12, 最終更新日: 2024-05-22)

主引用文献

Morin, P.E.,Awrey, D.E.,Edwards, A.M.,Arrowsmith, C.H.
Elongation factor TFIIS contains three structural domains: solution structure of domain II.
Proc.Natl.Acad.Sci.USA, 93:10604-10608, 1996

PubMed Abstract: Transcription elongation by RNA polymerase II is regulated by the general elongation factor TFIIS. This factor stimulates RNA polymerase II to transcribe through regions of DNA that promote the formation of stalled ternary complexes. Limited proteolytic digestion showed that yeast TFIIS is composed of three structural domains, termed I, II, and III. The two C-terminal domains (II and III) are required for transcription activity. The structure of domain III has been solved previously by using NMR spectroscopy. Here, we report the NMR-derived structure of domain II: a three-helix bundle built around a hydrophobic core composed largely of three tyrosines protruding from one face of the C-terminal helix. The arrangement of known inactivating mutations of TFIIS suggests that two surfaces of domain II are critical for transcription activity.

PubMed: 8855225
DOI: 10.1073/pnas.93.20.10604

実験手法

SOLUTION NMR