- EMDB-31217: The structure of ALC1 bound to the nucleosome -
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Basic information
Entry
Database: EMDB / ID: EMD-31217
Title
The structure of ALC1 bound to the nucleosome
Map data
The structure of ALC1 bound to the nucleosome
Sample
Complex: The structure of ALC1 bound to the nucleosome
Complex: ALC1
Protein or peptide: Chromodomain-helicase-DNA-binding protein 1-like
Complex: Histone
Protein or peptide: Histone H3.2
Protein or peptide: Histone H4
Protein or peptide: Histone H2A type 1
Protein or peptide: Histone H2B 1.1
Complex: DNA
DNA: DNA (167-MER)
DNA: DNA (167-MER)
Ligand: ADENOSINE-5'-DIPHOSPHATE
Ligand: BERYLLIUM TRIFLUORIDE ION
Function / homology
Function and homology information
poly-ADP-D-ribose modification-dependent protein binding / ATP-dependent chromatin remodeler activity / site of DNA damage / nucleosome binding / histone reader activity / DNA helicase activity / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / Dual Incision in GG-NER / Formation of Incision Complex in GG-NER / structural constituent of chromatin ...poly-ADP-D-ribose modification-dependent protein binding / ATP-dependent chromatin remodeler activity / site of DNA damage / nucleosome binding / histone reader activity / DNA helicase activity / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / Dual Incision in GG-NER / Formation of Incision Complex in GG-NER / structural constituent of chromatin / nucleosome / nucleosome assembly / site of double-strand break / chromatin remodeling / protein heterodimerization activity / DNA repair / nucleotide binding / DNA damage response / ATP hydrolysis activity / DNA binding / nucleoplasm / ATP binding / nucleus / plasma membrane / cytosol Similarity search - Function
Journal: Nat Commun / Year: 2021 Title: Structural basis of ALC1/CHD1L autoinhibition and the mechanism of activation by the nucleosome. Authors: Li Wang / Kangjing Chen / Zhucheng Chen / Abstract: Chromatin remodeler ALC1 (amplification in liver cancer 1) is crucial for repairing damaged DNA. It is autoinhibited and activated by nucleosomal epitopes. However, the mechanisms by which ALC1 is ...Chromatin remodeler ALC1 (amplification in liver cancer 1) is crucial for repairing damaged DNA. It is autoinhibited and activated by nucleosomal epitopes. However, the mechanisms by which ALC1 is regulated remain unclear. Here we report the crystal structure of human ALC1 and the cryoEM structure bound to the nucleosome. The structure shows the macro domain of ALC1 binds to lobe 2 of the ATPase motor, sequestering two elements for nucleosome recognition, explaining the autoinhibition mechanism of the enzyme. The H4 tail competes with the macro domain for lobe 2-binding, explaining the requirement for this nucleosomal epitope for ALC1 activation. A dual-arginine-anchor motif of ALC1 recognizes the acidic pocket of the nucleosome, which is critical for chromatin remodeling in vitro. Together, our findings illustrate the structures of ALC1 and shed light on its regulation mechanisms, paving the way for the discovery of drugs targeting ALC1 for the treatment of cancer.
History
Deposition
Apr 18, 2021
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Header (metadata) release
Jul 14, 2021
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Map release
Jul 14, 2021
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Update
Jul 14, 2021
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Current status
Jul 14, 2021
Processing site: PDBj / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
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