5ZZM

E. coli 50S subunit bound HflX protein in presence of ATP (AMP-PNP) and GTP (GMP-PNP) analogs.

5ZZM の概要

• エントリーDOI: 10.2210/pdb5zzm/pdb
• 関連するPDBエントリー: 5ADY
• EMDBエントリー: 6979
• 分子名称: GTPase HflX, 5S rRNA, 23S rRNA (3 entities in total)
• 機能のキーワード: atpase, rna helicase, heat stress, ribosome
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 1028489.27

構造登録者

Dey, S. (登録日: 2018-06-03, 公開日: 2018-06-27, 最終更新日: 2024-03-27)

主引用文献

Dey, S.,Biswas, C.,Sengupta, J.
The universally conserved GTPase HflX is an RNA helicase that restores heat-damagedEscherichia coliribosomes.
J. Cell Biol., 217:2519-2529, 2018

PubMed Abstract: The ribosome-associated GTPase HflX acts as an antiassociation factor upon binding to the 50S ribosomal subunit during heat stress in Although HflX is recognized as a guanosine triphosphatase, several studies have shown that the N-terminal domain 1 of HflX is capable of hydrolyzing adenosine triphosphate (ATP), but the functional role of its adenosine triphosphatase (ATPase) activity remains unknown. We demonstrate that HflX possesses ATP-dependent RNA helicase activity and is capable of unwinding large subunit ribosomal RNA. A cryo-electron microscopy structure of the 50S-HflX complex in the presence of nonhydrolyzable analogues of ATP and guanosine triphosphate hints at a mode of action for the RNA helicase and suggests the linker helical domain may have a determinant role in RNA unwinding. Heat stress results in inactivation of the ribosome, and we show that HflX can restore heat-damaged ribosomes and improve cell survival.

PubMed: 29930203
DOI: 10.1083/jcb.201711131

実験手法

ELECTRON MICROSCOPY (8.1 Å)