5FM7

Double-heterohexameric rings of full-length Rvb1(ADP)Rvb2(ADP)

5FM7 の概要

• エントリーDOI: 10.2210/pdb5fm7/pdb
• 関連するPDBエントリー: 5FLV 5FM6
• 分子名称: RVB1, RVB2, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: atp binding protein
• 由来する生物種: CHAETOMIUM THERMOPHILUM; 詳細
• 細胞内の位置: Nucleus : G0RYI5 G0RYC2
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 104775.25

構造登録者

Silva-Martin, N.,Dauden, M.I.,Glatt, S.,Hoffmann, N.A.,Mueller, C.W. (登録日: 2015-11-02, 公開日: 2016-01-20, 最終更新日: 2024-01-10)

主引用文献

Silva-Martin, N.,Dauden, M.I.,Glatt, S.,Hoffmann, N.A.,Kastritis, P.,Bork, P.,Beck, M.,Muller, C.W.
The Combination of X-Ray Crystallography and Cryo-Electron Microscopy Provides Insight Into the Overall Architecture of the Dodecameric Rvb1/Rvb2 Complex.
Plos One, 11:46457-, 2016

PubMed Abstract: The Rvb1/Rvb2 complex is an essential component of many cellular pathways. The Rvb1/Rvb2 complex forms a dodecameric assembly where six copies of each subunit form two heterohexameric rings. However, due to conformational variability, the way the two rings pack together is still not fully understood. Here, we present the crystal structure and two cryo-electron microscopy reconstructions of the dodecameric, full-length Rvb1/Rvb2 complex, all showing that the interaction between the two heterohexameric rings is mediated through the Rvb1/Rvb2-specific domain II. Two conformations of the Rvb1/Rvb2 dodecamer are present in solution: a stretched conformation also present in the crystal, and a compact conformation. Novel asymmetric features observed in the reconstruction of the compact conformation provide additional insight into the plasticity of the Rvb1/Rvb2 complex.

PubMed: 26745716
DOI: 10.1371/JOURNAL.PONE.0146457

実験手法

X-RAY DIFFRACTION (2.901 Å)