› 2jty

Solution NMR

Self-complemented variant of FimA, the main subunit of type 1 pilus

Released:
DOI: 10.2210/pdb2jty/pdb
PDB entry 2jty coloured by chain, ensemble of 20 models, front view.
PDB entry 2jty coloured by chain, ensemble of 20 models, side view.
PDB entry 2jty coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia coli
Primary publication:
Structure, folding and stability of FimA, the main structural subunit of type 1 pili from uropathogenic Escherichia coli strains.
Puorger C, Vetsch M, Wider G, Glockshuber R
J Mol Biol 412 520-35 (2011)
PMID: 21816158

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137417 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Type-1 fimbrial protein, A chain Chain: A
Molecule details ›
Chain: A
Length: 184 amino acids
Theoretical weight: 18.03 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P04128 (Residues: 24-182; Coverage: 100%)
Gene names: JW4277, b4314, fimA, pilA
Sequence domains: Fimbrial protein
Structure domains: Fimbrial-type adhesion domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 91%
Refinement method: torsion angle dynamics, molecular dynamics
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Immunoglobulin domains in Escherichia coli and other enterobacteria: from pathogenesis to applications in antibody technologies.
Bodelón et al. (2013)
2 more

12 mentions without citation

Modelling of pH-dependence to develop a strategy for stabilising mAbs at acidic steps in production.
Hebditch et al. (2020)
11 more