› 2ro0

Solution NMR

Solution structure of the knotted tudor domain of the yeast histone acetyltransferase, Esa1

Released:
DOI: 10.2210/pdb2ro0/pdb
PDB entry 2ro0 coloured by chain, ensemble of 20 models, front view.
PDB entry 2ro0 coloured by chain, ensemble of 20 models, side view.
PDB entry 2ro0 coloured by chain, ensemble of 20 models, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Novel structural and functional mode of a knot essential for RNA binding activity of the Esa1 presumed chromodomain.
Shimojo H, Sano N, Moriwaki Y, Okuda M, Horikoshi M, Nishimura Y
J Mol Biol 378 987-1001 (2008)
PMID: 18407291

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170671 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone acetyltransferase ESA1 Chain: A
Molecule details ›
Chain: A
Length: 92 amino acids
Theoretical weight: 10.79 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q08649 (Residues: 1-89; Coverage: 20%)
Gene names: ESA1, O5257, YOR244W
Sequence domains: RNA binding activity-knot of a chromodomain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

RNA regulation of epigenetic processes.
Mattick et al. (2009)
7 more

3 mentions without citation

Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectives.
Andreoli et al. (2013)
2 more