4YGY

Crystal Structure of Human Scp1 bound to trans-proline peptidomimetic CTD phospho-Ser5 peptide

4YGY の概要

• エントリーDOI: 10.2210/pdb4ygy/pdb
• 関連するPDBエントリー: 4YGX 4YH1
• 分子名称: Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1, peptidomimetic CTD phospho-Ser5 peptide, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: phosphatase, peptidomimetic, complex, hydrolase
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Nucleus : Q9GZU7
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 45714.07

構造登録者

Mayfield, J.E.,Zhang, Y. (登録日: 2015-02-26, 公開日: 2015-09-16, 最終更新日: 2024-11-20)

主引用文献

Mayfield, J.E.,Fan, S.,Wei, S.,Zhang, M.,Li, B.,Ellington, A.D.,Etzkorn, F.A.,Zhang, Y.J.
Chemical Tools To Decipher Regulation of Phosphatases by Proline Isomerization on Eukaryotic RNA Polymerase II.
Acs Chem.Biol., 10:2405-2414, 2015

PubMed Abstract: Proline isomerization greatly impacts biological signaling but is subtle and difficult to detect in proteins. We characterize this poorly understood regulatory mechanism for RNA polymerase II carboxyl terminal domain (CTD) phosphorylation state using novel, direct, and quantitative chemical tools. We determine the proline isomeric preference of three CTD phosphatases: Ssu72 as cis-proline specific, Scp1 and Fcp1 as strongly trans-preferred. Due to this inherent characteristic, these phosphatases respond differently to enzymes that catalyze the isomerization of proline, like Ess1/Pin1. We demonstrate that this selective regulation of RNA polymerase II phosphorylation state exists within human cells, consistent with in vitro assays. These results support a model in which, instead of a global enhancement of downstream enzymatic activities, proline isomerases selectively boost the activity of a subset of CTD regulatory factors specific for cis-proline. This leads to diversified phosphorylation states of CTD in vitro and in cells. We provide the chemical tools to investigate proline isomerization and its ability to selectively enhance signaling in transcription and other biological contexts.

PubMed: 26332362
DOI: 10.1021/acschembio.5b00296

実験手法

X-RAY DIFFRACTION (2.36 Å)