3RTX

Crystal structure of mammalian capping enzyme (Mce1) and Pol II CTD complex

3RTX の概要

• エントリーDOI: 10.2210/pdb3rtx/pdb
• 関連するPDBエントリー: 1I9S 1I9T
• 分子名称: mRNA-capping enzyme, RNA Polymerase II C-terminal domain, GUANINE, ... (4 entities in total)
• 機能のキーワード: guanylyltransferase, rna polymerase ii ctd, lysyl-n-gmp, nucleus, mrna capping, transferase
• 由来する生物種: Mus musculus (mouse); 詳細
• 細胞内の位置: Nucleus: O55236
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 81397.20

構造登録者

Ghosh, A.,Lima, C.D. (登録日: 2011-05-04, 公開日: 2011-06-29, 最終更新日: 2024-10-30)

主引用文献

Ghosh, A.,Shuman, S.,Lima, C.D.
Structural insights to how mammalian capping enzyme reads the CTD code.
Mol.Cell, 43:299-310, 2011

PubMed Abstract: Physical interaction between the phosphorylated RNA polymerase II carboxyl-terminal domain (CTD) and cellular capping enzymes is required for efficient formation of the 5' mRNA cap, the first modification of nascent mRNA. Here, we report the crystal structure of the RNA guanylyltransferase component of mammalian capping enzyme (Mce) bound to a CTD phosphopeptide. The CTD adopts an extended β-like conformation that docks Tyr1 and Ser5-PO(4) onto the Mce nucleotidyltransferase domain. Structure-guided mutational analysis verified that the Mce-CTD interface is a tunable determinant of CTD binding and stimulation of guanylyltransferase activity, and of Mce function in vivo. The location and composition of the CTD binding site on mammalian capping enzyme is distinct from that of a yeast capping enzyme that recognizes the same CTD primary structure. Thus, capping enzymes from different taxa have evolved different strategies to read the CTD code.

PubMed: 21683636
DOI: 10.1016/j.molcel.2011.06.001

実験手法

X-RAY DIFFRACTION (2.81 Å)