› 7xez

Solution NMR

NMR solution structures of p300 TAZ2 domain in complex with BRD4-NUT F1c domain binding motif #2

Released:
DOI: 10.2210/pdb7xez/pdb
PDB entry 7xez coloured by chain, ensemble of 20 models, front view.
PDB entry 7xez coloured by chain, ensemble of 20 models, side view.
PDB entry 7xez coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural mechanism of BRD4-NUT and p300 bipartite interaction in propagating aberrant gene transcription in chromatin in NUT carcinoma.
Yu D, Liang Y, Kim C, Jaganathan A, Ji D, Han X, Yang X, Jia Y, Gu R, Wang C, Zhang Q, Cheung KL, Zhou MM, Zeng L
Nat Commun 14 378 (2023)
PMID: 36690674

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-199928 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone acetyltransferase p300; NUT family member 1 Chain: A
Molecule details ›
Chain: A
Length: 163 amino acids
Theoretical weight: 17.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q09472 (Residues: 1723-1812; Coverage: 4%)
  • Canonical: Q86Y26 (Residues: 419-470; Coverage: 5%)
Gene names: C15orf55, EP300, NUT, NUTM1, P300
Sequence domains: TAZ zinc finger

Ligands and Environments

1 bound ligand:
Ligand ZN 3 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 83%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Onco-condensates: formation, multi-component organization, and biological functions.
Xu et al. (2023)
2 more