4U4C

The molecular architecture of the TRAMP complex reveals the organization and interplay of its two catalytic activities

4U4C の概要

• エントリーDOI: 10.2210/pdb4u4c/pdb
• 分子名称: ATP-dependent RNA helicase DOB1, Protein AIR2,Poly(A) RNA polymerase protein 2, SULFATE ION, ... (8 entities in total)
• 機能のキーワード: helicase, atpase, poly(a)polymerase, rna degradation, exosome, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• 細胞内の位置: Nucleus: P47047 P53632
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 127772.81

構造登録者

Falk, S.,Weir, J.R.,Hentschel, J.,Reichelt, P.,Bonneau, F.,Conti, E. (登録日: 2014-07-23, 公開日: 2014-09-24, 最終更新日: 2023-12-20)

主引用文献

Falk, S.,Weir, J.R.,Hentschel, J.,Reichelt, P.,Bonneau, F.,Conti, E.
The Molecular Architecture of the TRAMP Complex Reveals the Organization and Interplay of Its Two Catalytic Activities.
Mol.Cell, 55:856-867, 2014

PubMed Abstract: The TRAMP complex is involved in the nuclear surveillance and turnover of noncoding RNAs and intergenic transcripts. TRAMP is associated with the nuclear exosome and consists of a poly(A)polymerase subcomplex (Trf4-Air2) and a helicase (Mtr4). We found that N-terminal low-complexity regions of Trf4 and Air2 bind Mtr4 in a cooperative manner. The 2.4 Å resolution crystal structure of the corresponding ternary complex reveals how Trf4 and Air2 wrap around the DExH core of the helicase. Structure-based mutations on the DExH core impair binding to Trf4 and Air2, and also to Trf5 and Air1. The combination of structural, biochemical, and biophysical data suggests that the poly(A)polymerase core of Trf4-Air2 is positioned below the base of the helicase, where the unwound 3' end of an RNA substrate is expected to emerge. The results reveal conceptual similarities between the two major regulators of the exosome, the nuclear TRAMP and cytoplasmic Ski complexes.

PubMed: 25175027
DOI: 10.1016/j.molcel.2014.07.020

実験手法

X-RAY DIFFRACTION (2.4 Å)