› 1qjh

X-ray diffraction
2.2Å 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/pdb1qjh/pdb
PDB entry 1qjh coloured by chain, front view.
PDB entry 1qjh coloured by chain, side view.
PDB entry 1qjh 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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149939 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Small ribosomal subunit protein bS6 Chain: A
Molecule details ›
Chain: A
Length: 101 amino acids
Theoretical weight: 11.83 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

1 bound ligand:
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P42212
Unit cell:
a: 49.701Å b: 49.701Å c: 73.255Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.205 0.275
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)