› 5iay

Solution NMR

NMR structure of UHRF1 Tandem Tudor Domains in a complex with Spacer peptide

Released:
DOI: 10.2210/pdb5iay/pdb
PDB entry 5iay coloured by chain, ensemble of 20 models, front view.
PDB entry 5iay coloured by chain, ensemble of 20 models, side view.
PDB entry 5iay coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Hemi-methylated DNA opens a closed conformation of UHRF1 to facilitate its histone recognition.
Fang J, Cheng J, Wang J, Zhang Q, Liu M, Gong R, Wang P, Zhang X, Feng Y, Lan W, Gong Z, Tang C, Wong J, Yang H, Cao C, Xu Y
Nat Commun 7 11197 (2016)
PMID: 27045799

Function and Biology Details

Reaction catalysed: 
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188768 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase UHRF1 Chain: A
Molecule details ›
Chain: A
Length: 152 amino acids
Theoretical weight: 17.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96T88 (Residues: 134-285; Coverage: 19%)
Gene names: ICBP90, NP95, RNF106, UHRF1
Sequence domains: Tandem tudor domain within UHRF1
Structure domains:
E3 ubiquitin-protein ligase UHRF1 Chain: B
Molecule details ›
Chain: B
Length: 16 amino acids
Theoretical weight: 1.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96T88 (Residues: 642-657; Coverage: 2%)
Gene names: ICBP90, NP95, RNF106, UHRF1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 64%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

24 review citations

Allosteric control of mammalian DNA methyltransferases - a new regulatory paradigm.
Jeltsch et al. (2016)
23 more

1 mention without citation

Hemi-methylated DNA opens a closed conformation of UHRF1 to facilitate its histone recognition.
Fang et al. (2016)