4EP7

Functional implications from the Cid1 poly(U) polymerase crystal structure

4EP7 の概要

• エントリーDOI: 10.2210/pdb4ep7/pdb
• 分子名称: Poly(A) RNA polymerase protein cid1, URIDINE 5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: poly(u) polymerase, utp binding, transferase
• 由来する生物種: Schizosaccharomyces pombe (Fission yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 79081.74

構造登録者

Munoz-Tello, P.,Gabus, C.,Thore, S. (登録日: 2012-04-17, 公開日: 2012-06-06, 最終更新日: 2024-02-28)

主引用文献

Munoz-Tello, P.,Gabus, C.,Thore, S.
Functional implications from the cid1 poly(u) polymerase crystal structure.
Structure, 20:977-986, 2012

PubMed Abstract: In eukaryotes, mRNA degradation begins with poly(A) tail removal, followed by decapping, and the mRNA body is degraded by exonucleases. In recent years, the major influence of 3'-end uridylation as a regulatory step within several RNA degradation pathways has generated significant attention toward the responsible enzymes, which are called poly(U) polymerases (PUPs). We determined the atomic structure of the Cid1 protein, the founding member of the PUP family, in its UTP-bound form, allowing unambiguous positioning of the UTP molecule. Our data also suggest that the RNA substrate accommodation and product translocation by the Cid1 protein rely on local and global movements of the enzyme. Supplemented by point mutations, the atomic model is used to propose a catalytic cycle. Our study underlines the Cid1 RNA binding properties, a feature with critical implications for miRNAs, histone mRNAs, and, more generally, cellular RNA degradation.

PubMed: 22608966
DOI: 10.1016/j.str.2012.04.006

実験手法

X-RAY DIFFRACTION (2.2805 Å)