4PN1

Structure of S. pombe Pct1 RNA triphosphatase in complex with the Spt5 CTD

4PN1 の概要

• エントリーDOI: 10.2210/pdb4pn1/pdb
• 関連するPDBエントリー: 4PN0
• 分子名称: mRNA-capping enzyme subunit beta, Synthetic peptide, FORMIC ACID, ... (5 entities in total)
• 機能のキーワード: mrna triphosphatase, hydrolase, polynucleotide 5' triphosphatase, mrna processing, mrna capping, dimer, transcription elongation factor, hydrolase-transcription regulator complex, hydrolase/transcription regulator
• 由来する生物種: Schizosaccharomyces pombe (Fission yeast); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 150369.59

構造登録者

Lima, C.D.,Doamekpor, S.K. (登録日: 2014-05-22, 公開日: 2014-11-12, 最終更新日: 2023-09-27)

主引用文献

Doamekpor, S.K.,Schwer, B.,Sanchez, A.M.,Shuman, S.,Lima, C.D.
Fission yeast RNA triphosphatase reads an Spt5 CTD code.
Rna, 21:113-123, 2015

PubMed Abstract: mRNA capping enzymes are directed to nascent RNA polymerase II (Pol2) transcripts via interactions with the carboxy-terminal domains (CTDs) of Pol2 and transcription elongation factor Spt5. Fission yeast RNA triphosphatase binds to the Spt5 CTD, comprising a tandem repeat of nonapeptide motif TPAWNSGSK. Here we report the crystal structure of a Pct1·Spt5-CTD complex, which revealed two CTD docking sites on the Pct1 homodimer that engage TPAWN segments of the motif. Each Spt5 CTD interface, composed of elements from both subunits of the homodimer, is dominated by van der Waals contacts from Pct1 to the tryptophan of the CTD. The bound CTD adopts a distinctive conformation in which the peptide backbone makes a tight U-turn so that the proline stacks over the tryptophan. We show that Pct1 binding to Spt5 CTD is antagonized by threonine phosphorylation. Our results fortify an emerging concept of an "Spt5 CTD code" in which (i) the Spt5 CTD is structurally plastic and can adopt different conformations that are templated by particular cellular Spt5 CTD receptor proteins; and (ii) threonine phosphorylation of the Spt5 CTD repeat inscribes a binary on-off switch that is read by diverse CTD receptors, each in its own distinctive manner.

PubMed: 25414009
DOI: 10.1261/rna.048181.114

実験手法

X-RAY DIFFRACTION (2.803 Å)