1SZA

The RNA polymerase II CTD in mRNA processing: beta-turn recognition and beta-spiral model

1SZA の概要

• エントリーDOI: 10.2210/pdb1sza/pdb
• 関連するPDBエントリー: 1SZ9
• 分子名称: PCF11 protein, CTD-peptide (3 entities in total)
• 機能のキーワード: pcf11, rna polymerase ii ctd interacting domain, arm repeats, phosphoserine, transcription
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• 細胞内の位置: Nucleus : P39081
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 51409.91

構造登録者

Meinhart, A.,Cramer, P. (登録日: 2004-04-05, 公開日: 2004-07-13, 最終更新日: 2024-10-16)

主引用文献

Meinhart, A.,Cramer, P.
Recognition of RNA polymerase II carboxy-terminal domain by 3'-RNA-processing factors.
Nature, 430:223-226, 2004

PubMed Abstract: During transcription, RNA polymerase (Pol) II synthesizes eukaryotic messenger RNA. Transcription is coupled to RNA processing by the carboxy-terminal domain (CTD) of Pol II, which consists of up to 52 repeats of the sequence Tyr 1-Ser 2-Pro 3-Thr 4-Ser 5-Pro 6-Ser 7 (refs 1, 2). After phosphorylation, the CTD binds tightly to a conserved CTD-interacting domain (CID) present in the proteins Pcf11 and Nrd1, which are essential and evolutionarily conserved factors for polyadenylation-dependent and -independent 3'-RNA processing, respectively. Here we describe the structure of a Ser 2-phosphorylated CTD peptide bound to the CID domain of Pcf11. The CTD motif Ser 2-Pro 3-Thr 4-Ser 5 forms a beta-turn that binds to a conserved groove in the CID domain. The Ser 2 phosphate group does not make direct contact with the CID domain, but may be recognized indirectly because it stabilizes the beta-turn with an additional hydrogen bond. Iteration of the peptide structure results in a compact beta-spiral model of the CTD. The model suggests that, during the mRNA transcription-processing cycle, compact spiral regions in the CTD are unravelled and regenerated in a phosphorylation-dependent manner.

PubMed: 15241417
DOI: 10.1038/nature02679

実験手法

X-RAY DIFFRACTION (2.2 Å)