3EEU

Structure of the RNA pyrophosphohydrolase BdRppH in complex with Holmium

3EEU の概要

• エントリーDOI: 10.2210/pdb3eeu/pdb
• 関連するPDBエントリー: 3EES
• 分子名称: Probable pyrophosphohydrolase, HOLMIUM ATOM, ACETATE ION, ... (5 entities in total)
• 機能のキーワード: nudix, rna pyrophosphohydrolase, hydrolase
• 由来する生物種: Bdellovibrio bacteriovorus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35752.03

構造登録者

Messing, S.A.,Gabelli, S.B.,Amzel, L.M. (登録日: 2008-09-05, 公開日: 2009-03-24, 最終更新日: 2024-02-21)

主引用文献

Messing, S.A.,Gabelli, S.B.,Liu, Q.,Celesnik, H.,Belasco, J.G.,Pineiro, S.A.,Amzel, L.M.
Structure and Biological Function of the RNA Pyrophosphohydrolase BdRppH from Bdellovibrio bacteriovorus.
Structure, 17:472-481, 2009

PubMed Abstract: Until recently, the mechanism of mRNA decay in bacteria was thought to be different from that of eukaryotes. This paradigm changed with the discovery that RppH (ORF176/NudH/YgdP), an Escherichia coli enzyme that belongs to the Nudix superfamily, is an RNA pyrophosphohydrolase that initiates mRNA decay by cleaving pyrophosphate from the 5'-triphosphate. Here we report the 1.9 Angstroms resolution structure of the Nudix hydrolase BdRppH from Bdellovibrio bacteriovorus, a bacterium that feeds on other Gram-negative bacteria. Based on the structure of the enzyme alone and in complex with GTP-Mg2+, we propose a mode of RNA binding similar to that of the nuclear decapping enzyme from Xenopus laevis, X29. In additional experiments, we show that BdRppH can indeed function in vitro and in vivo as an RNA pyrophosphohydrolase. These findings set the basis for the identification of possible decapping enzymes in other bacteria.

PubMed: 19278661
DOI: 10.1016/j.str.2008.12.022

実験手法

X-RAY DIFFRACTION (2 Å)