7KKF

Crystal Structure of S. cerevisiae Ess1

7KKF の概要

• エントリーDOI: 10.2210/pdb7kkf/pdb
• 関連するPDBエントリー: 1PIN 1YW5
• 分子名称: Peptidyl-prolyl cis-trans isomerase ESS1 (2 entities in total)
• 機能のキーワード: ess1, prolyl isomerase, transcription, isomerase
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 38743.31

構造登録者

Namitz, K.E.W.,Alicea-Velazquez, N.L.,Cosgrove, M.S.,Hanes, S.D. (登録日: 2020-10-27, 公開日: 2021-03-31, 最終更新日: 2023-10-18)

主引用文献

Namitz, K.E.W.,Zheng, T.,Canning, A.J.,Alicea-Velazquez, N.L.,Castaneda, C.A.,Cosgrove, M.S.,Hanes, S.D.
Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism.
Commun Biol, 4:398-398, 2021

PubMed Abstract: Accurate gene transcription in eukaryotes depends on isomerization of serine-proline bonds within the carboxy-terminal domain (CTD) of RNA polymerase II. Isomerization is part of the "CTD code" that regulates recruitment of proteins required for transcription and co-transcriptional RNA processing. Saccharomyces cerevisiae Ess1 and its human ortholog, Pin1, are prolyl isomerases that engage the long heptad repeat (YSPTSPS) of the CTD by an unknown mechanism. Here, we used an integrative structural approach to decipher Ess1 interactions with the CTD. Ess1 has a rigid linker between its WW and catalytic domains that enforces a distance constraint for bivalent interaction with the ends of long CTD substrates (≥4-5 heptad repeats). Our binding results suggest that the Ess1 WW domain anchors the proximal end of the CTD substrate during isomerization, and that linker divergence may underlie evolution of substrate specificity.

PubMed: 33767358
DOI: 10.1038/s42003-021-01906-8

実験手法

X-RAY DIFFRACTION (2.4 Å)