1RO4

RDC-derived models of the zinc ribbon domain of human general transcription factor TFIIB (zinc free structures)

1RO4 の概要

• エントリーDOI: 10.2210/pdb1ro4/pdb
• 関連するPDBエントリー: 1RLY
• 分子名称: Transcription initiation factor IIB (1 entity in total)
• 機能のキーワード: zinc ribbon, rubredoxin knuckle, metal binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: Q00403
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6571.42

構造登録者

Ghosh, M.,Ikura, M. (登録日: 2003-12-01, 公開日: 2004-05-25, 最終更新日: 2024-05-22)

主引用文献

Ghosh, M.,Elsby, L.M.,Mal, T.K.,Gooding, J.M.,Roberts, S.G.,Ikura, M.
Probing Zn2+-binding effects on the zinc-ribbon domain of human general transcription factor TFIIB.
Biochem.J., 378:317-324, 2004

PubMed Abstract: The general transcription factor, TFIIB, plays an important role in the assembly of the pre-initiation complex. The N-terminal domain (NTD) of TFIIB contains a zinc-ribbon motif, which is responsible for the recruitment of RNA polymerase II and TFIIF to the core promoter region. Although zinc-ribbon motif structures of eukaryotic and archaeal TFIIBs have been reported previously, the structural role of Zn2 binding to TFIIB remains to be determined. In the present paper, we report NMR and biochemical studies of human TFIIB NTD, which characterize the structure and dynamics of the TFIIB Zn2-binding domain in both Zn2-bound and -free states. The NMR data show that, whereas the backbone fold of NTD is pre-formed in the apo state, Zn2 binding reduces backbone mobility in the b-turn (Arg28-Gly30), induces enhanced structural rigidity of the charged-cluster domain in the central linker region of TFIIB and appends a positive surface charge within the Zn2-binding site. V8 protease-sensitivity assays of full-length TFIIB support the Zn2-dependent structural changes. These structural effects of Zn2 binding on TFIIB may have a critical role in interactions with its binding partners, such as the Rpb1 subunit of RNA polymerase II.

PubMed: 14641108
DOI: 10.1042/BJ20031706

実験手法

SOLUTION NMR