5OAF

Human Rvb1/Rvb2 heterohexamer in INO80 complex

Summary for 5OAF

• Entry DOI: 10.2210/pdb5oaf/pdb
• EMDB information: 3772 3773
• Descriptor: RuvB-like 1, RuvB-like 2, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: chromatin remodelling complex, gene regulation
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 6
• Total formula weight: 307121.34

Authors

Aramayo, R.J.,Bythell-Douglas, R.,Ayala, R.,Willhoft, O.,Wigley, D.,Zhang, X. (deposition date: 2017-06-21, release date: 2017-12-13, Last modification date: 2024-05-15)

Primary citation

Aramayo, R.J.,Willhoft, O.,Ayala, R.,Bythell-Douglas, R.,Wigley, D.B.,Zhang, X.
Cryo-EM structures of the human INO80 chromatin-remodeling complex.
Nat. Struct. Mol. Biol., 25:37-44, 2018

PubMed Abstract: Access to chromatin for processes such as transcription and DNA repair requires the sliding of nucleosomes along DNA. This process is aided by chromatin-remodeling complexes, such as the multisubunit INO80 chromatin-remodeling complex. Here we present cryo-EM structures of the active core complex of human INO80 at 9.6 Å, with portions at 4.1-Å resolution, and reconstructions of combinations of subunits. Together, these structures reveal the architecture of the INO80 complex, including Ino80 and actin-related proteins, which is assembled around a single RUVBL1 (Tip49a) and RUVBL2 (Tip49b) AAA+ heterohexamer. An unusual spoked-wheel structural domain of the Ino80 subunit is engulfed by this heterohexamer; both, in combination, form the core of the complex. We also identify a cleft in RUVBL1 and RUVBL2, which forms a major interaction site for partner proteins and probably communicates these interactions to its nucleotide-binding sites.

PubMed: 29323271
DOI: 10.1038/s41594-017-0003-7

Experimental method

ELECTRON MICROSCOPY (4.06 Å)