› 3u5o

X-ray diffraction
2.7Å resolution

Crystal structure of the complex of TRIM33 PHD-Bromo and H3(1-22)K9me3K14acK18ac histone peptide

Released:
DOI: 10.2210/pdb3u5o/pdb
PDB entry 3u5o coloured by chain, front view.
PDB entry 3u5o coloured by chain, side view.
PDB entry 3u5o coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A poised chromatin platform for TGF-β access to master regulators.
Xi Q, Wang Z, Zaromytidou AI, Zhang XH, Chow-Tsang LF, Liu JX, Kim H, Barlas A, Manova-Todorova K, Kaartinen V, Studer L, Mark W, Patel DJ, Massagué J
Cell 147 1511-24 (2011)
PMID: 22196728

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:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159451 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase TRIM33 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 207 amino acids
Theoretical weight: 23.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9UPN9 (Residues: 882-1087; Coverage: 18%)
Gene names: KIAA1113, RFG7, TIF1G, TRIM33
Sequence domains:
Structure domains:
Histone H3.1 Chains: I, J, K, L, M, N, O, P
Molecule details ›
Chains: I, J, K, L, M, N, O, P
Length: 22 amino acids
Theoretical weight: 2.49 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P68431 (Residues: 2-23; Coverage: 16%)
Gene names: H3C1, H3C10, H3C11, H3C12, H3C2, H3C3, H3C4, H3C6, H3C7, H3C8, H3FA, H3FB, H3FC HIST1H3C, H3FD, H3FF, H3FH, H3FI, H3FJ, H3FK, H3FL, HIST1H3A, HIST1H3B, HIST1H3D, HIST1H3E, HIST1H3F, HIST1H3G, HIST1H3H, HIST1H3I, HIST1H3J

Ligands and Environments

1 bound ligand:
Ligand ZN 16 x ZN
2 modified residues:
Ligand M3L 8 x M3L
Ligand ALY 16 x ALY

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P1
Unit cell:
a: 63.639Å b: 63.65Å c: 125.195Å
α: 90.05° β: 89.98° γ: 89.93°
R-values:
R R work R free
0.207 0.205 0.28
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

78 review citations

Molecular mechanisms of epithelial-mesenchymal transition.
Lamouille et al. (2014)
77 more

9 mentions without citation

Readout of epigenetic modifications.
Patel et al. (2013)
8 more