9T4V

ALC1/CHD1L in an intermediate conformation, bound to a PARylated nucleosome

This is a non-PDB format compatible entry.

Summary for 9T4V

• Entry DOI: 10.2210/pdb9t4v/pdb
• EMDB information: 13065 55533
• Descriptor: Histone H3.2, Histone H4, Histone H2A type 1, ... (7 entities in total)
• Functional Keywords: alc1, chd1l, chromatin remodeler, dna damage response, nucleosome, poly(adp-ribose), dna binding protein
• Biological source: Xenopus laevis (African clawed frog); More
• Total number of polymer chains: 11
• Total formula weight: 306814.43

Authors

Bridges, H.R.,Bacic, L.,Deindl, S.,Gaullier, G. (deposition date: 2025-11-02, release date: 2025-11-19, Last modification date: 2026-05-27)

Primary citation

Bridges, H.R.,Bacic, L.,Deindl, S.,Gaullier, G.
Cryo-EM structure of ALC1 in an open conformation bound to a PARylated nucleosome.
Acta Crystallogr D Struct Biol, 2026

PubMed Abstract: Nucleosomes are the repeating unit of chromatin. They act as recognition platforms for chromatin-binding factors that coordinate genome maintenance. The chromatin remodeler Amplified in Liver Cancer 1 (ALC1) is a key component of the DNA-damage response and a promising therapeutic target in cancer. Through extensive classification of our previously deposited cryo-electron microscopy dataset, we identified a previously unresolved ALC1-nucleosome complex characterized by a more open conformation of ALC1. This is the first structure of ALC1 in which all domains are visualized in the context of a nucleosome complex, including the regulatory macro domain and a single α-helix motif within the linker. This newly identified conformation may represent an intermediate between the auto-inhibited and active states, and provides new structural insights into the conformational transitions that regulate the activity of ALC1.

PubMed: 42159202
DOI: 10.1107/S2059798326004158

Experimental method

ELECTRON MICROSCOPY (6.6 Å)