5YGU

Crystal structure of Escherichia coli (strain K12) mRNA Decapping Complex RppH-DapF

5YGU の概要

• エントリーDOI: 10.2210/pdb5ygu/pdb
• 分子名称: Diaminopimelate epimerase, RNA pyrophosphohydrolase, L(+)-TARTARIC ACID, ... (5 entities in total)
• 機能のキーワード: rpph-dapf, decapping, hydrolase, isomerase-hydrolase complex, isomerase/hydrolase
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51986.40

構造登録者

Wang, Q.,Guan, Z.Y.,Zhang, D.L.,Zou, T.T.,Yin, P. (登録日: 2017-09-27, 公開日: 2018-06-06, 最終更新日: 2023-11-22)

主引用文献

Wang, Q.,Zhang, D.,Guan, Z.,Li, D.,Pei, K.,Liu, J.,Zou, T.,Yin, P.
DapF stabilizes the substrate-favoring conformation of RppH to stimulate its RNA-pyrophosphohydrolase activity in Escherichia coli.
Nucleic Acids Res., 46:6880-6892, 2018

PubMed Abstract: mRNA decay is an important strategy by which bacteria can rapidly adapt to their ever-changing surroundings. The 5'-terminus state of mRNA determines the velocity of decay of many types of RNA. In Escherichia coli, RNA pyrophosphohydrolase (RppH) is responsible for the removal of the 5'-terminal triphosphate from hundreds of mRNAs and triggers its rapid degradation by ribonucleases. A diaminopimelate epimerase, DapF, can directly interact with RppH and stimulate its hydrolysis activity in vivo and in vitro. However, the molecular mechanism remains to be elucidated. Here, we determined the complex structure of DapF-RppH as a heterotetramer in a 2:2 molar ratio. DapF-bound RppH exhibits an RNA-favorable conformation similar to the RNA-bound state, suggesting that association with DapF promotes and stabilizes RppH in a conformation that facilitates substrate RNA binding and thus stimulates the activity of RppH. To our knowledge, this is the first published structure of an RNA-pyrophosphohydrolysis complex in bacteria. Our study provides a framework for further investigation of the potential regulators involved in the RNA-pyrophosphohydrolysis process in prokaryotes.

PubMed: 29931175
DOI: 10.1093/nar/gky528

実験手法

X-RAY DIFFRACTION (2.298 Å)