4XWT

Crystal structure of RNase J complexed with UMP

4XWT の概要

• エントリーDOI: 10.2210/pdb4xwt/pdb
• 関連するPDBエントリー: 4xww
• 分子名称: DR2417, ZINC ION, MANGANESE (II) ION, ... (6 entities in total)
• 機能のキーワード: ribonuclease, two-metal-ion, dimerization, manganese, deinococcus radiodurans, rna binding protein
• 由来する生物種: Deinococcus radiodurans
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 124606.82

構造登録者

Lu, M.,Zhang, H.,Xu, Q.,Hua, Y.,Zhao, Y. (登録日: 2015-01-29, 公開日: 2015-12-16, 最終更新日: 2024-03-20)

主引用文献

Zhao, Y.,Lu, M.,Zhang, H.,Hu, J.,Zhou, C.,Xu, Q.,Shah, A.M.U.H.,Xu, H.,Wang, L.,Hua, Y.
Structural insights into catalysis and dimerization enhanced exonuclease activity of RNase J
Nucleic Acids Res., 43:5550-5559, 2015

PubMed Abstract: RNase J is a conserved ribonuclease that belongs to the β-CASP family of nucleases. It possesses both endo- and exo-ribonuclease activities, which play a key role in pre-rRNA maturation and mRNA decay. Here we report high-resolution crystal structures of Deinococcus radiodurans RNase J complexed with RNA or uridine 5'-monophosphate in the presence of manganese ions. Biochemical and structural studies revealed that RNase J uses zinc ions for two-metal-ion catalysis. One residue conserved among RNase J orthologues (motif B) forms specific electrostatic interactions with the scissile phosphate of the RNA that is critical for the catalysis and product stabilization. The additional manganese ion, which is coordinated by conserved residues at the dimer interface, is critical for RNase J dimerization and exonuclease activity. The structures may also shed light on the mechanism of RNase J exo- and endonucleolytic activity switch.

PubMed: 25940620
DOI: 10.1093/nar/gkv444

実験手法

X-RAY DIFFRACTION (2.003 Å)