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TitleThe cryo-EM structure of human UHRF1 bound to mononucleosomes.
Journal, issue, pagesTo Be Published
Publish dateMar 9, 2025 (structure data deposition date)
AuthorsNaschberger A / Baradaran R / Sayed A / Fischle W
External linksSearch PubMed
MethodsEM (single particle)
Resolution2.8 - 4.7 Å
Structure data

EMDB-63669: Consensus map of human UHRF1 bound to mononucleosome with hemimethylated DNA at superhelical location -6.2.
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-63670: The focused refinement map of the TTD-PHD domain of UHRF1 bound to a mononucleosome with hemimethylated DNA at superhelical location -6.2.
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-63671: The SRA domain of human UHRF1 bound to a mononucleosome with hemimethylated DNA at superhelical location -6.2.
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-63672: The RING domain of human UHRF1 bound to a mononucleosome in its pre-active state.
Method: EM (single particle) / Resolution: 4.7 Å

EMDB-63673: Human UHRF1 bound to a mononucleosome with hemimethylated DNA at superhelical location -5.6.
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-63674: Human UHRF1 bound to a mononucleosome with hemimethylation at superhelical location -6.2 and a Histone H3K9me3 methylation mark.
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-63675: Human UHRF1 bound to a mononucleosome with a hemimethylation site in the linker DNA.
Method: EM (single particle) / Resolution: 3.7 Å

63676

9m76

EMDB-63676, PDB-9m76:
UHRF1 bound to a mononucleosome in its pre-active state, with the RING domain bound to the SRA domain.
Method: EM (single particle) / Resolution: 4.1 Å

63677

9m77

EMDB-63677, PDB-9m77:
The activated state of human UHRF1 bound to a mononucleosome, with the finger loop ordered and linker 4 disordered.
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • xenopus laevis (African clawed frog)
  • homo sapiens (human)
KeywordsDNA BINDING PROTEIN / Epigenetic reader/writer protein involved in DNA methylation.

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