› 1zdx

Solution NMR

Solution Structure of the type 1 pilus assembly platform FimD(25-125)

Released:
DOI: 10.2210/pdb1zdx/pdb
PDB entry 1zdx coloured by chain, ensemble of 20 models, front view.
PDB entry 1zdx coloured by chain, ensemble of 20 models, side view.
PDB entry 1zdx coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia coli
Primary publication:
Structural basis of chaperone-subunit complex recognition by the type 1 pilus assembly platform FimD.
Nishiyama M, Horst R, Eidam O, Herrmann T, Ignatov O, Vetsch M, Bettendorff P, Jelesarov I, Grütter MG, Wüthrich K, Glockshuber R, Capitani G
EMBO J 24 2075-86 (2005)
PMID: 15920478

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-151645 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Outer membrane usher protein FimD Chain: A
Molecule details ›
Chain: A
Length: 101 amino acids
Theoretical weight: 10.87 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P30130 (Residues: 70-170; Coverage: 12%)
Gene names: JW5780, b4317, fimD
Sequence domains: PapC N-terminal domain
Structure domains: Ubiquitin-like (UB roll)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

20 review citations

Evolution of the chaperone/usher assembly pathway: fimbrial classification goes Greek.
Nuccio et al. (2007)
19 more

3 mentions without citation

The bacterial outer membrane β-barrel assembly machinery.
Kim et al. (2012)
2 more