› 1nil

Solution NMR

A COMPARISON OF NMR SOLUTION STRUCTURES OF THE RECEPTOR BINDING DOMAINS OF PSEUDOMONAS AERUGINOSA PILI STRAINS PAO, KB7, AND PAK: IMPLICATIONS FOR RECEPTOR BINDING AND SYNTHETIC VACCINE DESIGN

Released:
DOI: 10.2210/pdb1nil/pdb
PDB entry 1nil coloured by chain, front view.
PDB entry 1nil coloured by chain, side view.
PDB entry 1nil coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Comparison of NMR solution structures of the receptor binding domains of Pseudomonas aeruginosa pili strains PAO, KB7, and PAK: implications for receptor binding and synthetic vaccine design.
Campbell AP, McInnes C, Hodges RS, Sykes BD
Biochemistry 34 16255-68 (1995)
PMID: 8845350

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136422 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fimbrial protein Chain: A
Molecule details ›
Chain: A
Length: 18 amino acids
Theoretical weight: 1.94 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Not provided
UniProt:
  • Canonical: P02973 (Residues: 134-150; Coverage: 11%)
Gene names: fimA, pilA

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

3 review citations

Boehringer Mannheim award lecture 1995. La conference Boehringer Mannheim 1995. De novo design of alpha-helical proteins: basic research to medical applications.
Hodges RS. (1996)
2 more

2 mentions without citation

Single-residue changes in the C-terminal disulfide-bonded loop of the Pseudomonas aeruginosa type IV pilin influence pilus assembly and twitching motility.
Harvey et al. (2009)
1 more