5A0T

Catalysis and 5' end sensing by ribonuclease RNase J of the metallo- beta-lactamase family

5A0T の概要

• エントリーDOI: 10.2210/pdb5a0t/pdb
• 関連するPDBエントリー: 5A0V
• 分子名称: RIBONUCLEASE J, 5'-R(*CP*GP*CP*CP*UP)-3', DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• 機能のキーワード: hydrolase-rna complex, ribonuclease, rnase j, endonuclease, exonuclease, hydrolase/rna
• 由来する生物種: STREPTOMYCES COELICOLOR A3(2); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 126420.34

構造登録者

Pei, X.Y.,Bralley, P.,Jones, G.H.,Luisi, B.F. (登録日: 2015-04-22, 公開日: 2015-08-19, 最終更新日: 2024-01-10)

主引用文献

Pei, X.Y.,Bralley, P.,Jones, G.H.,Luisi, B.F.
Linkage of Catalysis and 5' End Recognition in Ribonuclease Rnase J
Nucleic Acids Res., 43:8066-, 2015

PubMed Abstract: In diverse bacterial species, the turnover and processing of many RNAs is mediated by the ribonuclease RNase J, a member of the widely occurring metallo-β-lactamase enzyme family. We present crystal structures of Streptomyces coelicolor RNase J with bound RNA in pre- and post-cleavage states, at 2.27 Å and 2.80 Å resolution, respectively. These structures reveal snapshots of the enzyme cleaving substrate directionally and sequentially from the 5' terminus. In the pre-cleavage state, a water molecule is coordinated to a zinc ion pair in the active site but is imperfectly oriented to launch a nucleophilic attack on the phosphate backbone. A conformational switch is envisaged that enables the in-line positioning of the attacking water and may be facilitated by magnesium ions. Adjacent to the scissile bond, four bases are stacked in a tightly sandwiching pocket, and mutagenesis results indicate that this organization helps to drive processive exo-ribonucleolytic cleavage. Like its numerous homologues, S. coelicolor RNase J can also cleave some RNA internally, and the structural data suggest how the preference for exo- versus endo-cleavage mode is linked with recognition of the chemical status of the substrate's 5' end.

PubMed: 26253740
DOI: 10.1093/NAR/GKV732

実験手法

X-RAY DIFFRACTION (2.283 Å)