› 1nfj

X-ray diffraction
2Å resolution

Structure of a Sir2 substrate, alba, reveals a mechanism for deactylation-induced enhancement of DNA-binding

Released:
DOI: 10.2210/pdb1nfj/pdb
PDB entry 1nfj coloured by chain, front view.
PDB entry 1nfj coloured by chain, side view.
PDB entry 1nfj coloured by chain, top view.
Source organism: Archaeoglobus fulgidus
Primary publication:
Structure of a Sir2 substrate, Alba, reveals a mechanism for deacetylation-induced enhancement of DNA binding.
Zhao K, Chai X, Marmorstein R
J Biol Chem 278 26071-7 (2003)
PMID: 12730210

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128011 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA/RNA-binding protein Alba 2 Chain: A
Molecule details ›
Chain: A
Length: 89 amino acids
Theoretical weight: 9.91 KDa
Source organism: Archaeoglobus fulgidus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O28323 (Residues: 1-89; Coverage: 100%)
Gene names: AF_1956, albA2
Sequence domains: Alba
Structure domains: Alba-like domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: I212121
Unit cell:
a: 33.835Å b: 56.026Å c: 90.268Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.242 0.226 0.256
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

11 review citations

The diverse superfamily of lysine acetyltransferases and their roles in leukemia and other diseases.
Yang XJ. (2004)
10 more

2 mentions without citation

Identification of the ligand binding sites on the molecular surface of proteins.
Kinoshita et al. (2005)
1 more