1I9S

CRYSTAL STRUCTURE OF THE RNA TRIPHOSPHATASE DOMAIN OF MOUSE MRNA CAPPING ENZYME

1I9S の概要

• エントリーDOI: 10.2210/pdb1i9s/pdb
• 関連するPDBエントリー: 1I9T
• 分子名称: MRNA CAPPING ENZYME, SULFATE ION, CACODYLATE ION, ... (6 entities in total)
• 機能のキーワード: rna triphosphatase domain, mrna capping enzyme, hydrolase
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Nucleus: O55236
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24697.18

構造登録者

Changela, A.,Ho, C.K.,Martins, A.,Shuman, S.,Mondragon, A. (登録日: 2001-03-20, 公開日: 2001-05-23, 最終更新日: 2024-02-07)

主引用文献

Changela, A.,Ho, C.K.,Martins, A.,Shuman, S.,Mondragon, A.
Structure and mechanism of the RNA triphosphatase component of mammalian mRNA capping enzyme.
EMBO J., 20:2575-2586, 2001

PubMed Abstract: The 5' capping of mammalian pre-mRNAs is initiated by RNA triphosphatase, a member of the cysteine phosphatase superfamily. Here we report the 1.65 A crystal structure of mouse RNA triphosphatase, which reveals a deep, positively charged active site pocket that can fit a 5' triphosphate end. Structural, biochemical and mutational results show that despite sharing an HCxxxxxR(S/T) motif, a phosphoenzyme intermediate and a core alpha/beta-fold with other cysteine phosphatases, the mechanism of phosphoanhydride cleavage by mammalian capping enzyme differs from that used by protein phosphatases to hydrolyze phosphomonoesters. The most significant difference is the absence of a carboxylate general acid catalyst in RNA triphosphatase. Residues conserved uniquely among the RNA phosphatase subfamily are important for function in cap formation and are likely to play a role in substrate recognition.

PubMed: 11350947
DOI: 10.1093/emboj/20.10.2575

実験手法

X-RAY DIFFRACTION (1.65 Å)