5M9D

Solution structure of Rtt103 CTD-interacting domain bound to a Ser2Ser7 phosphorylated CTD peptide

5M9D の概要

• エントリーDOI: 10.2210/pdb5m9d/pdb
• NMR情報: BMRB: 34058
• 分子名称: Regulator of Ty1 transposition protein 103, THR-SER-PRO-SEP-TYR-SEP-PRO-THR-SER-PRO-SEP-TYR-SEP-PRO-THR-SER (2 entities in total)
• 機能のキーワード: transcription, rnapii c-terminal domain, ctd-interacting domain, phosphorylation
• 由来する生物種: Saccharomyces cerevisiae S288c; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18534.69

構造登録者

Jasnovidova, O.,Kubicek, K.,Stefl, R. (登録日: 2016-11-01, 公開日: 2017-10-11, 最終更新日: 2024-11-20)

主引用文献

Jasnovidova, O.,Klumpler, T.,Kubicek, K.,Kalynych, S.,Plevka, P.,Stefl, R.
Structure and dynamics of the RNAPII CTDsome with Rtt103.
Proc. Natl. Acad. Sci. U.S.A., 114:11133-11138, 2017

PubMed Abstract: RNA polymerase II contains a long C-terminal domain (CTD) that regulates interactions at the site of transcription. The CTD architecture remains poorly understood due to its low sequence complexity, dynamic phosphorylation patterns, and structural variability. We used integrative structural biology to visualize the architecture of the CTD in complex with Rtt103, a 3'-end RNA-processing and transcription termination factor. Rtt103 forms homodimers via its long coiled-coil domain and associates densely on the repetitive sequence of the phosphorylated CTD via its N-terminal CTD-interacting domain. The CTD-Rtt103 association opens the compact random coil structure of the CTD, leading to a beads-on-a-string topology in which the long rod-shaped Rtt103 dimers define the topological and mobility restraints of the entire assembly. These findings underpin the importance of the structural plasticity of the CTD, which is templated by a particular set of CTD-binding proteins.

PubMed: 29073019
DOI: 10.1073/pnas.1712450114

実験手法

SOLUTION NMR