1Z60

Solution structure of the carboxy-terminal domain of human TFIIH P44 subunit

「1E53」から置き換えられました

1Z60 の概要

• エントリーDOI: 10.2210/pdb1z60/pdb
• 分子名称: TFIIH basal transcription factor complex p44 subunit, ZINC ION (2 entities in total)
• 機能のキーワード: basic transcription factor, zinc binding protein, ring finger, transcription
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: Q13888
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6826.35

構造登録者

Kellenberger, E.,Dominguez, C.,Fribourg, S.,Wasielewski, E.,Moras, D.,Poterszman, A.,Boelens, R.,Kieffer, B. (登録日: 2005-03-21, 公開日: 2005-04-12, 最終更新日: 2024-05-29)

主引用文献

Kellenberger, E.,Dominguez, C.,Fribourg, S.,Wasielewski, E.,Moras, D.,Poterszman, A.,Boelens, R.,Kieffer, B.
Solution structure of the C-terminal domain of TFIIH P44 subunit reveals a novel type of C4C4 ring domain involved in protein-protein interactions.
J.Biol.Chem., 280:20785-20792, 2005

PubMed Abstract: The human general transcription factor TFIIH is involved in both transcription and DNA nucleotide excision repair. Among the 10 subunits of the complex, p44 subunit plays a crucial role in both mechanisms. Its N-terminal domain interacts with the XPD helicase, whereas its C-terminal domain is involved specifically in the promoter escape activity. By mutating an exposed and non-conserved cysteine residue into a serine, we produced a soluble mutant of p44-(321-395) suitable for solution structure determination. The domain adopts a C4C4 RING domain structure with sequential organization of beta-strands that is related to canonical RING domains by a circular permutation of the beta-sheet elements. Analysis of the molecular surface and mutagenesis experiments suggests that the binding of p44-(321-395) to TFIIH p34 subunit is not mediated by electrostatic interactions and, thus, differs from previously reported interaction mechanisms involving RING domains.

PubMed: 15790571
DOI: 10.1074/jbc.M412999200

実験手法

SOLUTION NMR