3T3O

Molecular basis for the recognition and cleavage of RNA (CUGG) by the bifunctional 5'-3' exo/endoribonuclease RNase J

3T3O の概要

• エントリーDOI: 10.2210/pdb3t3o/pdb
• 関連するPDBエントリー: 3BK1 3BK2 3T3N
• 分子名称: Metal dependent hydrolase, O2'methyl-RNA, ZINC ION, ... (5 entities in total)
• 機能のキーワード: protein-rna complex, metallo-beta-lactamase, rnase j, endoribonuclease, 5'-3' exoribonuclease, metal dependent hydrolase, rna, hydrolase, hydrolase-rna complex, hydrolase/rna
• 由来する生物種: Thermus thermophilus HB27; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64388.95

構造登録者

Dorleans, A.,Li de la Sierra-Gallay, I.,Piton, J.,Zig, L.,Gilet, L.,Putzer, H.,Condon, C. (登録日: 2011-07-25, 公開日: 2011-10-19, 最終更新日: 2024-02-28)

主引用文献

Dorleans, A.,Li de la Sierra-Gallay, I.,Piton, J.,Zig, L.,Gilet, L.,Putzer, H.,Condon, C.
Molecular Basis for the Recognition and Cleavage of RNA by the Bifunctional 5'-3' Exo/Endoribonuclease RNase J.
Structure, 19:1252-1261, 2011

PubMed Abstract: RNase J is a key member of the β-CASP family of metallo-β-lactamases involved in the maturation and turnover of RNAs in prokaryotes. The B. subtilis enzyme possesses both 5'-3' exoribonucleolytic and endonucleolytic activity, an unusual property for a ribonuclease. Here, we present the crystal structure of T. thermophilus RNase J bound to a 4 nucleotide RNA. The structure reveals an RNA-binding channel that illustrates how the enzyme functions in 5'-3' exoribonucleolytic mode and how it can function as an endonuclease. A second, negatively charged tunnel leads from the active site, and is ideally located to evacuate the cleaved nucleotide in 5'-3' exonucleolytic mode. We show that B. subtilis RNase J1, which shows processive behavior on long RNAs, behaves distributively for substrates less than 5 nucleotides in length. We propose a model involving the binding of the RNA to the surface of the β-CASP domain to explain the enzyme's processive action.

PubMed: 21893286
DOI: 10.1016/j.str.2011.06.018

実験手法

X-RAY DIFFRACTION (2.5 Å)