6fqa

X-ray diffraction
2.85Å resolution

Crystal structure of the CsuC-CsuA/B chaperone-subunit preassembly complex of the archaic chaperone-usher Csu pili of Acinetobacter baumannii

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Pili assembly chaperone N-terminal domain-containing protein Chains: A, C
Molecule details ›
Chains: A, C
Length: 243 amino acids
Theoretical weight: 27 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q6XBY4 (Residues: 35-277; Coverage: 88%)
Gene name: csuC
Sequence domains: Pili and flagellar-assembly chaperone, PapD N-terminal domain
Spore coat protein U domain-containing protein Chains: B, D
Molecule details ›
Chains: B, D
Length: 152 amino acids
Theoretical weight: 15.93 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q6XBY7 (Residues: 38-180; Coverage: 92%)
Gene name: csuA/B
Sequence domains: Spore Coat Protein U domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P6522
Unit cell:
a: 94.379Å b: 94.379Å c: 390.745Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.197 0.262
Expression system: Escherichia coli BL21