1F3U

CRYSTAL STRUCTURE OF THE RAP30/74 INTERACTION DOMAINS OF HUMAN TFIIF

1F3U の概要

• エントリーDOI: 10.2210/pdb1f3u/pdb
• 分子名称: TRANSCRIPTION INITIATION FACTOR IIF, BETA SUBUNIT, TRANSCRIPTION INITIATION FACTOR IIF, ALPHA SUBUNIT (3 entities in total)
• 機能のキーワード: general transcription initiation and elongation factor, rna polymerase ii, novel dimerization fold, beta barrel, transcription
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: P13984 P35269
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 130643.12

構造登録者

Gaiser, F.,Tan, S.,Richmond, T.J. (登録日: 2000-06-06, 公開日: 2000-10-11, 最終更新日: 2024-02-07)

主引用文献

Gaiser, F.,Tan, S.,Richmond, T.J.
Novel dimerization fold of RAP30/RAP74 in human TFIIF at 1.7 A resolution.
J.Mol.Biol., 302:1119-1127, 2000

PubMed Abstract: General transcription factor IIF (TFIIF) is required for transcription by RNA polymerase II; it consists minimally of a heterodimer of RNA polymerase-associated proteins RAP30 and RAP74. According to solution and mutagenesis studies, the multiple domains of RAP30 and RAP74 bind PolII, TFIIB, TAF250 and DNA in interactions that are essential for transcription initiation and elongation. The X-ray structure of the RAP30/RAP74 interaction domains at 1.7 A resolution reveals a novel "triple barrel" dimerization fold and suggests with mutant data that interactions with the transcription apparatus are mediated not only by this tripartite beta-barrel, but also via flexible loops and alpha and beta-structures extending from it.

PubMed: 11183778
DOI: 10.1006/jmbi.2000.4110

実験手法

X-RAY DIFFRACTION (1.7 Å)