2DB3

Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa

2DB3 の概要

• エントリーDOI: 10.2210/pdb2db3/pdb
• 分子名称: 5'-R(*UP*UP*UP*UP*UP*UP*UP*UP*UP*U)-3', ATP-dependent RNA helicase vasa, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: dead-box, helicase, protein-rna complex, atpase, riken structural genomics/proteomics initiative, rsgi, structural genomics, hydrolase-rna complex, hydrolase/rna
• 由来する生物種: Drosophila melanogaster (fruit fly)
• 細胞内の位置: Cytoplasm: P09052
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 207549.32

構造登録者

Sengoku, T.,Nureki, O.,Nakamura, A.,Kobayashi, S.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2005-12-14, 公開日: 2006-05-02, 最終更新日: 2024-03-13)

主引用文献

Sengoku, T.,Nureki, O.,Nakamura, A.,Kobayashi, S.,Yokoyama, S.
Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa.
Cell(Cambridge,Mass.), 125:287-300, 2006

PubMed Abstract: DEAD-box RNA helicases, which regulate various processes involving RNA, have two RecA-like domains as a catalytic core to alter higher-order RNA structures. We determined the 2.2 A resolution structure of the core of the Drosophila DEAD-box protein Vasa in complex with a single-stranded RNA and an ATP analog. The ATP analog intensively interacts with both of the domains, thereby bringing them into the closed form, with many interdomain interactions of conserved residues. The bound RNA is sharply bent, avoiding a clash with a conserved alpha helix in the N-terminal domain. This "wedge" helix should disrupt base pairs by bending one of the strands when a duplex is bound. Mutational analyses indicated that the interdomain interactions couple ATP hydrolysis to RNA unwinding, probably through fine positioning of the duplex relative to the wedge helix. This mechanism, which differs from those for canonical translocating helicases, may enable the targeted modulation of intricate RNA structures.

PubMed: 16630817
DOI: 10.1016/j.cell.2006.01.054

実験手法

X-RAY DIFFRACTION (2.2 Å)