› 1g1o

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF THE HIGHLY AMYLOIDOGENIC TRANSTHYRETIN MUTANT TTR G53S/E54D/L55S

Released:
DOI: 10.2210/pdb1g1o/pdb
PDB entry 1g1o coloured by chain, front view.
PDB entry 1g1o coloured by chain, side view.
PDB entry 1g1o coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The beta-slip: a novel concept in transthyretin amyloidosis.
Eneqvist T, Andersson K, Olofsson A, Lundgren E, Sauer-Eriksson AE
Mol Cell 6 1207-18 (2000)
PMID: 11106758

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-136168 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transthyretin Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 127 amino acids
Theoretical weight: 13.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P02766 (Residues: 21-147; Coverage: 100%)
Gene names: PALB, TTR
Sequence domains: HIUase/Transthyretin family
Structure domains: Transthyretin/hydroxyisourate hydrolase domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P3221
Unit cell:
a: 58.31Å b: 58.31Å c: 228.95Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.238 0.238 0.29
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Structures for amyloid fibrils.
Makin et al. (2005)
4 more

6 mentions without citation

Edge Strand Dissociation and Conformational Changes in Transthyretin under Amyloidogenic Conditions.
Childers et al. (2020)
5 more