› 1v1h

X-ray diffraction
1.9Å resolution

Adenovirus fibre shaft sequence N-terminally fused to the bacteriophage T4 fibritin foldon trimerisation motif with a short linker

Released:
DOI: 10.2210/pdb1v1h/pdb
PDB entry 1v1h coloured by chain, front view.
PDB entry 1v1h coloured by chain, side view.
PDB entry 1v1h coloured by chain, top view.
Source organisms:
Primary publication:
Adenovirus fibre shaft sequences fold into the native triple beta-spiral fold when N-terminally fused to the bacteriophage T4 fibritin foldon trimerisation motif.
Papanikolopoulou K, Teixeira S, Belrhali H, Forsyth VT, Mitraki A, van Raaij MJ
J Mol Biol 342 219-27 (2004)
PMID: 15313619

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136676 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fiber protein; Fibritin Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 103 amino acids
Theoretical weight: 10.79 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P03275 (Residues: 319-392; Coverage: 13%)
  • Canonical: P10104 (Residues: 456-484, 458-484; Coverage: 6%)
Gene names: L5, wac
Sequence domains: Adenoviral fibre protein (repeat/shaft region)
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: C2
Unit cell:
a: 77.77Å b: 183.33Å c: 58.97Å
α: 90° β: 129.29° γ: 90°
R-values:
R R work R free
0.182 0.182 0.24
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Unusual biophysics of intrinsically disordered proteins.
Uversky VN. (2013)
1 more

1 mention without citation

Adenovirus Fibers as Ultra-Stable Vehicles for Intracellular Nanoparticle and Protein Delivery.
Kokotidou et al. (2022)