2HX6

Solution structure analysis of the phage T4 endoribonuclease RegB

2HX6 の概要

• エントリーDOI: 10.2210/pdb2hx6/pdb
• 分子名称: Ribonuclease (1 entity in total)
• 機能のキーワード: alpha/beta fold, hydrolase
• 由来する生物種: Enterobacteria phage T4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17939.55

構造登録者

Odaert, B.,Saida, F.,Uzan, M.,Bontems, F. (登録日: 2006-08-02, 公開日: 2006-10-31, 最終更新日: 2024-05-29)

主引用文献

Odaert, B.,Saida, F.,Aliprandi, P.,Durand, S.,Crechet, J.B.,Guerois, R.,Laalami, S.,Uzan, M.,Bontems, F.
Structural and functional studies of RegB, a new member of a family of sequence-specific ribonucleases involved in mRNA inactivation on the ribosome.
J.Biol.Chem., 282:2019-2028, 2007

PubMed Abstract: The RegB endoribonuclease participates in the bacteriophage T4 life cycle by favoring early messenger RNA breakdown. RegB specifically cleaves GGAG sequences found in intergenic regions, mainly in translation initiation sites. Its activity is very low but can be enhanced up to 100-fold by the ribosomal 30 S subunit or by ribosomal protein S1. RegB has no significant sequence homology to any known protein. Here we used NMR to solve the structure of RegB and map its interactions with two RNA substrates. We also generated a collection of mutants affected in RegB function. Our results show that, despite the absence of any sequence homology, RegB has structural similarities with two Escherichia coli ribonucleases involved in mRNA inactivation on translating ribosomes: YoeB and RelE. Although these ribonucleases have different catalytic sites, we propose that RegB is a new member of the RelE/YoeB structural and functional family of ribonucleases specialized in mRNA inactivation within the ribosome.

PubMed: 17046813
DOI: 10.1074/jbc.M608271200

実験手法

SOLUTION NMR