4WW4

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

4WW4 の概要

• エントリーDOI: 10.2210/pdb4ww4/pdb
• 分子名称: RuvB-like 1, RuvB-like 2, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: aaa+ atpases, hexameric ring, dodecameric assemblies, full-length proteins, adp-bound states, hydrolase
• 由来する生物種: Chaetomium thermophilum; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 107245.92

構造登録者

Lakomek, K.,Hopfner, K.-P. (登録日: 2014-11-10, 公開日: 2015-02-18, 最終更新日: 2024-01-10)

主引用文献

Lakomek, K.,Stoehr, G.,Tosi, A.,Schmailzl, M.,Hopfner, K.P.
Structural Basis for Dodecameric Assembly States and Conformational Plasticity of the Full-Length AAA+ ATPases Rvb1Rvb2.
Structure, 23:483-495, 2015

PubMed Abstract: As building blocks of diverse macromolecular complexes, the AAA+ ATPases Rvb1 and Rvb2 are crucial for many cellular activities including cancer-related processes. Their oligomeric structure and function remain unclear. We report the crystal structures of full-length heteromeric Rvb1·Rvb2 complexes in distinct nucleotide binding states. Chaetomium thermophilum Rvb1·Rvb2 assemble into hexameric rings of alternating molecules and into stable dodecamers. Intriguingly, the characteristic oligonucleotide-binding (OB) fold domains (DIIs) of Rvb1 and Rvb2 occupy unequal places relative to the compact AAA+ core ring. While Rvb1's DII forms contacts between hexamers, Rvb2's DII is rotated 100° outward, occupying lateral positions. ATP was retained bound to Rvb1 but not Rvb2 throughout purification, suggesting nonconcerted ATPase activities and nucleotide binding. Significant conformational differences between nucleotide-free and ATP-/ADP-bound states in the crystal structures and in solution suggest that the functional role of Rvb1·Rvb2 is mediated by highly interconnected structural switches. Our structures provide an atomic framework for dodecameric states and Rvb1·Rvb2's conformational plasticity.

PubMed: 25661652
DOI: 10.1016/j.str.2014.12.015

実験手法

X-RAY DIFFRACTION (2.94 Å)