8B0J

CryoEM structure of bacterial RNaseE.RapZ.GlmZ complex central to the control of cell envelope biogenesis

8B0J の概要

• エントリーDOI: 10.2210/pdb8b0j/pdb
• EMDBエントリー: 15785
• 分子名称: RNase adapter protein RapZ, Ribonuclease E, GlmZ small RNA (3 entities in total)
• 機能のキーワード: endonuclease rnase e, adaptor protein rapz, small regulatory rna glmz, rna binding protein
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 325251.86

構造登録者

Islam, M.S.,Hardwick, H.W.,Chirgadze, D.Y.,Luisi, B.F. (登録日: 2022-09-07, 公開日: 2022-10-05, 最終更新日: 2025-07-02)

主引用文献

Islam, M.S.,Hardwick, S.W.,Quell, L.,Durica-Mitic, S.,Chirgadze, D.Y.,Gorke, B.,Luisi, B.F.
Structure of a bacterial ribonucleoprotein complex central to the control of cell envelope biogenesis.
Embo J., 42:e112574-e112574, 2023

PubMed Abstract: Biogenesis of the essential precursor of the bacterial cell envelope, glucosamine-6-phosphate (GlcN6P), is controlled by intricate post-transcriptional networks mediated by GlmZ, a small regulatory RNA (sRNA). GlmZ stimulates translation of the mRNA encoding GlcN6P synthtase in Escherichia coli, but when bound by RapZ protein, the sRNA becomes inactivated through cleavage by the endoribonuclease RNase E. Here, we report the cryoEM structure of the RapZ:GlmZ complex, revealing a complementary match of the RapZ tetrameric quaternary structure to structural repeats in the sRNA. The nucleic acid is contacted by RapZ mostly through a highly conserved domain that shares an evolutionary relationship with phosphofructokinase and suggests links between metabolism and riboregulation. We also present the structure of a precleavage intermediate formed between the binary RapZ:GlmZ complex and RNase E that reveals how GlmZ is presented and recognised by the enzyme. The structures provide a framework for understanding how other encounter complexes might guide recognition and action of endoribonucleases on target transcripts, and how structured substrates in polycistronic precursors may be recognised for processing by RNase E.

PubMed: 36504162
DOI: 10.15252/embj.2022112574

実験手法

ELECTRON MICROSCOPY (3.99 Å)