› 1tr8

X-ray diffraction
2.27Å resolution

Crystal Structure of archaeal Nascent Polypeptide-associated Complex (aeNAC)

Released:
DOI: 10.2210/pdb1tr8/pdb
PDB 1tr8 coloured by chain and viewed from the front.
PDB 1tr8 coloured by chain and viewed from the side.
PDB 1tr8 coloured by chain and viewed from the top.
Source organism: Methanothermobacter marburgensis
Primary publication:
The crystal structure of archaeal nascent polypeptide-associated complex (NAC) reveals a unique fold and the presence of a ubiquitin-associated domain.
Spreter T, Pech M, Beatrix B
J. Biol. Chem. 280 15849-54 (2005)
PMID: 15665334

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nascent polypeptide-associated complex protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 102 amino acids
Theoretical weight: 11.96 KDa
Source organism: Methanothermobacter marburgensis
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C0K9 (Residues: 19-117; Coverage: 85%)
Gene names: MTBMA_c06300, nac
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 18 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P43212
Unit cell:
a: 90.89Å b: 90.89Å c: 49.476Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.194 0.24
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Exploring the roles of basal transcription factor 3 in eukaryotic growth and development.
Jamil et al. (2015)
5 more

1 mention without citation

Ribosome association and stability of the nascent polypeptide-associated complex is dependent upon its own ubiquitination.
Panasenko et al. (2009)