1YQT

RNase-L Inhibitor

1YQT の概要

• エントリーDOI: 10.2210/pdb1yqt/pdb
• 分子名称: RNase l inhibitor, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: atp-binding cassette, ribosome biogenesis, hydrolyase-translation complex, hydrolyase/translation
• 由来する生物種: Pyrococcus furiosus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 62200.39

構造登録者

Karcher, A.,Buttner, K.,Martens, B.,Jansen, R.P.,Hopfner, K.P. (登録日: 2005-02-02, 公開日: 2005-04-19, 最終更新日: 2017-10-11)

主引用文献

Karcher, A.,Buttner, K.,Martens, B.,Jansen, R.P.,Hopfner, K.P.
X-ray structure of RLI, an essential twin cassette ABC ATPase involved in ribosome biogenesis and HIV capsid assembly.
Structure, 13:649-659, 2005

PubMed Abstract: The ABC ATPase RNase-L inhibitor (RLI) emerges as a key enzyme in ribosome biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. To help reveal the structural mechanism of RLI, we determined the Mg2+-ADP bound crystal structure of the twin cassette ATPase of P. furiosus RLI at 1.9 A resolution and analyzed functional motifs in yeast in vivo. RLI shows similarities but also differences to known ABC enzyme structures. Twin nucleotide binding domains (NBD1 and NBD2) are arranged to form two composite active sites in their interface cleft, indicating they undergo the ATP-driven clamp-like motion of the NBDs of ABC transporters. An unusual "hinge" domain along the NBD1:NBD2 interface provides a frame for association and possibly ATP-driven conformational changes of the NBDs. Our results establish a first structural basis for ABC domain heterodimers and suggest that RLI may act as mechanochemical enzyme in ribosome and HIV capsid biogenesis.

PubMed: 15837203
DOI: 10.1016/j.str.2005.02.008

実験手法

X-RAY DIFFRACTION (1.9 Å)