1EO0

CONSERVED DOMAIN COMMON TO TRANSCRIPTION FACTORS TFIIS, ELONGIN A, CRSP70

1EO0 の概要

• エントリーDOI: 10.2210/pdb1eo0/pdb
• 関連するPDBエントリー: 1ENW
• 分子名称: TRANSCRIPTION ELONGATION FACTOR S-II (1 entity in total)
• 機能のキーワード: helix-bundle, structural genomics, psi, protein structure initiative, northeast structural genomics consortium, nesg, 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: 8822.35

構造登録者

Booth, V.,Koth, C.,Edwards, A.M.,Arrowsmith, C.H.,Northeast Structural Genomics Consortium (NESG) (登録日: 2000-03-21, 公開日: 2000-05-03, 最終更新日: 2024-05-22)

主引用文献

Booth, V.,Koth, C.,Edwards, A.M.,Arrowsmith, C.H.
Structure of a conserved domain common to the transcription factors TFIIS, elongin A, and CRSP70
J.Biol.Chem., 275:31266-31268, 2000

PubMed Abstract: TFIIS is a transcription elongation factor that consists of three domains. We have previously solved the structures of domains II and III, which stimulate arrested polymerase II elongation complexes in order to resume transcription. Domain I is conserved in evolution from yeast to human species and is homologous to the transcription factors elongin A and CRSP70. Domain I also interacts with the transcriptionally active RNA polymerase II holoenzyme and therefore, may have a function unrelated to the previously described transcription elongation activity of TFIIS. We have solved the structure of domain I of yeast TFIIS using NMR spectroscopy. Domain I is a compact four-helix bundle that is structurally independent of domains II and III of the TFIIS. Using the yeast structure as a template, we have modeled the homologous domains from elongin A and CRSP70 and identified a conserved positively charged patch on the surface of all three proteins, which may be involved in conserved functional interactions with the transcriptional machinery.

PubMed: 10811649
DOI: 10.1074/jbc.M002595200

実験手法

SOLUTION NMR