5F6C

The structure of E. coli RNase E catalytically inactive mutant with RNA bound

5F6C の概要

• エントリーDOI: 10.2210/pdb5f6c/pdb
• 分子名称: Ribonuclease E, RNA (5'-R(P*GP*U)-3'), RNA (5'-R(P*GP*UP*G)-3'), ... (7 entities in total)
• 機能のキーワード: ribonuclease, hydrolytic mechanism, regulatory rna, hydrolase
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 117324.74

構造登録者

Bandyra, K.J.,Luisi, B.F. (登録日: 2015-12-05, 公開日: 2016-12-14, 最終更新日: 2024-05-08)

主引用文献

Bandyra, K.J.,Wandzik, J.M.,Luisi, B.F.
Substrate Recognition and Autoinhibition in the Central Ribonuclease RNase E.
Mol. Cell, 72:275-285.e4, 2018

PubMed Abstract: The endoribonuclease RNase E is a principal factor in RNA turnover and processing that helps to exercise fine control of gene expression in bacteria. While its catalytic activity can be strongly influenced by the chemical identity of the 5' end of RNA substrates, the enzyme can also cleave numerous substrates irrespective of the chemistry of their 5' ends through a mechanism that has remained largely unexplained. We report structural and functional data illuminating details of both operational modes. Our crystal structure of RNase E in complex with the sRNA RprA reveals a duplex recognition site that saddles an inter-protomer surface to help present substrates for cleavage. Our data also reveal an autoinhibitory pocket that modulates the overall activity of the ribonuclease. Taking these findings together, we propose how RNase E uses versatile modes of RNA recognition to achieve optimal activity and specificity.

PubMed: 30270108
DOI: 10.1016/j.molcel.2018.08.039

実験手法

X-RAY DIFFRACTION (3.002 Å)