2NUE

Crystal structure of RNase III from Aquifex aeolicus complexed with ds-RNA at 2.9-Angstrom Resolution

2NUE の概要

• エントリーDOI: 10.2210/pdb2nue/pdb
• 関連するPDBエントリー: 1RC7 1YYO 1YYW 1YZ9 2EZ6 2NUF 2NUG
• 分子名称: 46-MER, Ribonuclease III (3 entities in total)
• 機能のキーワード: ribonuclease iii, dsrna, rna interference, endonucleolytic cleavage, hydrolase-rna complex, hydrolase/rna
• 由来する生物種: Aquifex aeolicus
• 細胞内の位置: Cytoplasm : O67082
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 67113.60

構造登録者

Gan, J.H.,Shaw, G.,Tropea, J.E.,Waugh, D.S.,Court, D.L.,Ji, X. (登録日: 2006-11-09, 公開日: 2007-11-20, 最終更新日: 2023-08-30)

主引用文献

Gan, J.,Shaw, G.,Tropea, J.E.,Waugh, D.S.,Court, D.L.,Ji, X.
A stepwise model for double-stranded RNA processing by ribonuclease III.
Mol.Microbiol., 67:143-154, 2007

PubMed Abstract: RNA interference is mediated by small interfering RNAs produced by members of the ribonuclease III (RNase III) family represented by bacterial RNase III and eukaryotic Rnt1p, Drosha and Dicer. For mechanistic studies, bacterial RNase III has been a valuable model system for the family. Previously, we have shown that RNase III uses two catalytic sites to create the 2-nucleotide (nt) 3' overhangs in its products. Here, we present three crystal structures of RNase III in complex with double-stranded RNA, demonstrating how Mg(2+) is essential for the formation of a catalytically competent protein-RNA complex, how the use of two Mg(2+) ions can drive the hydrolysis of each phosphodiester bond, and how conformational changes in both the substrate and the protein are critical elements for assembling the catalytic complex. Moreover, we have modelled a protein-substrate complex and a protein-reaction intermediate (transition state) complex on the basis of the crystal structures. Together, the crystal structures and the models suggest a stepwise mechanism for RNase III to execute the phosphoryl transfer reaction.

PubMed: 18047582
DOI: 10.1111/j.1365-2958.2007.06032.x

実験手法

X-RAY DIFFRACTION (2.9 Å)