› 1p5u

X-ray diffraction
1.99Å resolution

X-ray structure of the ternary Caf1M:Caf1:Caf1 chaperone:subunit:subunit complex

Released:
DOI: 10.2210/pdb1p5u/pdb
PDB entry 1p5u coloured by chain, front view.
PDB entry 1p5u coloured by chain, side view.
PDB entry 1p5u coloured by chain, top view.
Source organism: Yersinia pestis
Primary publication:
Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: preserved folding energy drives fiber formation.
Zavialov AV, Berglund J, Pudney AF, Fooks LJ, Ibrahim TM, MacIntyre S, Knight SD
Cell 113 587-96 (2003)
PMID: 12787500

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150880 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Chaperone protein caf1M Chain: A
Molecule details ›
Chain: A
Length: 235 amino acids
Theoretical weight: 26.33 KDa
Source organism: Yersinia pestis
Expression system: Escherichia coli
UniProt:
  • Canonical: P26926 (Residues: 24-258; Coverage: 99%)
Gene names: Y1098, YPMT1.82, YP_pMT084, caf1M
Sequence domains:
Structure domains: Immunoglobulins
F1 capsule antigen Chain: B
Molecule details ›
Chain: B
Length: 149 amino acids
Theoretical weight: 15.66 KDa
Source organism: Yersinia pestis
Expression system: Escherichia coli
UniProt:
  • Canonical: P26948 (Residues: 22-170; Coverage: 100%)
Gene names: Y1100, YPMT1.84, YP_pMT082, caf1
Sequence domains: Caf1 Capsule antigen
Structure domains: Fimbrial-type adhesion domain
F1 capsule antigen Chain: C
Molecule details ›
Chain: C
Length: 147 amino acids
Theoretical weight: 15.67 KDa
Source organism: Yersinia pestis
Expression system: Escherichia coli
UniProt:
  • Canonical: P26948 (Residues: 35-170; Coverage: 91%)
Gene names: Y1100, YPMT1.84, YP_pMT082, caf1
Sequence domains: Caf1 Capsule antigen
Structure domains: Fimbrial-type adhesion domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21212
Unit cell:
a: 178.816Å b: 69.62Å c: 45.271Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.166 0.216
Expression system: Escherichia coli

Quick links

Citations

34 review citations

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

12 mentions without citation

Structural bioinformatic analysis of DsbA proteins and their pathogenicity associated substrates.
Santos-Martin et al. (2021)
11 more