› 3q35

X-ray diffraction
3.3Å resolution

Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated histone acetylation

Released:
DOI: 10.2210/pdb3q35/pdb
Model geometry
Fit model/data
PDB entry 3q35 coloured by chain, front view.
PDB entry 3q35 coloured by chain, side view.
PDB entry 3q35 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated histone acetylation.
Tang Y, Holbert MA, Delgoshaie N, Wurtele H, Guillemette B, Meeth K, Yuan H, Drogaris P, Lee EH, Durette C, Thibault P, Verreault A, Cole PA, Marmorstein R
Structure 19 221-31 (2011)
PMID: 21256037

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156892 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone acetyltransferase RTT109 Chain: A
Molecule details ›
Chain: A
Length: 438 amino acids
Theoretical weight: 50.35 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q07794 (Residues: 1-436; Coverage: 100%)
Gene names: KAT11, KIM2, L1377, REM50, RTT109, YLL002W
Sequence domains: Histone acetylation protein
Vacuolar protein sorting-associated protein 75 Chain: B
Molecule details ›
Chain: B
Length: 232 amino acids
Theoretical weight: 27.29 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P53853 (Residues: 1-232; Coverage: 88%)
Gene names: N0890, VPS75, YNL246W
Sequence domains: Nucleosome assembly protein (NAP)

Ligands and Environments


Cofactor: Ligand ACO 1 x ACO
1 bound ligand:
Ligand EDO 1 x EDO
1 modified residue:
Ligand ALY 1 x ALY

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P21212
Unit cell:
a: 98.085Å b: 119.001Å c: 80.292Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.207 0.248
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

Writers and readers of histone acetylation: structure, mechanism, and inhibition.
Marmorstein et al. (2014)
7 more

11 mentions without citation

Histone chaperone networks shaping chromatin function.
Hammond et al. (2017)
10 more