› 1cqn

X-ray diffraction
2.1Å resolution

PROTEIN AGGREGATION AND ALZHEIMER'S DISEASE: CRYSTALLOGRAPHIC ANALYSIS OF THE PHENOMENON. ENGINEERED VERSION OF THE RIBOSOMAL PROTEIN S6 USED AS A STABLE SCAFFOLD TO STUDY OLIGOMERIZATION.

Released:
DOI: 10.2210/pdb1cqn/pdb
PDB entry 1cqn coloured by chain, front view.
PDB entry 1cqn coloured by chain, side view.
PDB entry 1cqn coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: a structural clue to amyloid assembly.
Otzen DE, Kristensen O, Oliveberg M
Proc Natl Acad Sci U S A 97 9907-12 (2000)
PMID: 10944185

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149938 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Small ribosomal subunit protein bS6 Chains: A, B
Molecule details ›
Chains: A, B
Length: 101 amino acids
Theoretical weight: 11.91 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: P23370 (Residues: 1-101; Coverage: 100%)
Gene names: rps6, rpsF
Sequence domains: Ribosomal protein S6
Structure domains: Alpha-Beta Plaits

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P6422
Unit cell:
a: 82.821Å b: 82.821Å c: 141.583Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.218 0.218 0.276
Expression system: Escherichia coli

Quick links

Citations

20 review citations

Protein misfolding, functional amyloid, and human disease.
Chiti et al. (2006)
19 more

1 mention without citation

Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: a structural clue to amyloid assembly.
Otzen et al. (2000)