2NUB

Structure of Aquifex aeolicus Argonuate

2NUB の概要

• エントリーDOI: 10.2210/pdb2nub/pdb
• 分子名称: Argonaute (2 entities in total)
• 機能のキーワード: rnaseh, argonaute, ribonuclease, rnai, risc, signaling protein
• 由来する生物種: Aquifex aeolicus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 83264.37

構造登録者

Rashid, U.J.,Paterok, D.,Koglin, A.,Gohlke, H.,Piehler, J.,Chen, J.C.-H. (登録日: 2006-11-09, 公開日: 2007-02-06, 最終更新日: 2023-10-25)

主引用文献

Rashid, U.J.,Paterok, D.,Koglin, A.,Gohlke, H.,Piehler, J.,Chen, J.C.
Structure of Aquifex aeolicus argonaute highlights conformational flexibility of the PAZ domain as a potential regulator of RNA-induced silencing complex function.
J.Biol.Chem., 282:13824-13832, 2007

PubMed Abstract: Gene silencing mediated by RNA interference requires the sequence-specific recognition of target mRNA by the endonuclease Argonaute, the primary enzymatic component of the RNA-induced silencing complex. We report the crystal structure of Aquifex aeolicus Argonaute, refined at 3.2A resolution. Relative to recent Argonaute structures, a 24 degrees reorientation of the PAZ domain in our structure opens a basic cleft between the N-terminal and PAZ domains, exposing the guide strand binding pocket of PAZ. This rearrangement leads to a branched, Y-shaped system of grooves that extends through the molecule and merges in a central channel containing the catalytic residues. A 5.5-ns molecular dynamics simulation of Argonaute shows a strong tendency of the PAZ and N-terminal domains to be mobile. Binding of single-stranded DNA to Argonaute monitored by total internal reflection fluorescence spectroscopy shows biphasic kinetics, also indicative of domain rearrangement upon DNA binding. Conformational rearrangement of the PAZ domain may therefore be critical for the catalytic cycle of Argonaute and the RNA-induced silencing complex.

PubMed: 17130125
DOI: 10.1074/jbc.M608619200

実験手法

X-RAY DIFFRACTION (3.2 Å)