› 1qpp

X-ray diffraction
2.6Å resolution

CRYSTAL STRUCTURES OF SELF CAPPING PAPD CHAPERONE HOMODIMERS

Released:
DOI: 10.2210/pdb1qpp/pdb
PDB entry 1qpp coloured by chain, front view.
PDB entry 1qpp coloured by chain, side view.
PDB entry 1qpp coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural basis of chaperone self-capping in P pilus biogenesis.
Hung DL, Pinkner JS, Knight SD, Hultgren SJ
Proc Natl Acad Sci U S A 96 8178-83 (1999)
PMID: 10393968

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147317 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperone protein PapD Chains: A, B
Molecule details ›
Chains: A, B
Length: 218 amino acids
Theoretical weight: 24.49 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P15319 (Residues: 22-239; Coverage: 100%)
Gene name: papD
Sequence domains:
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: P21212
Unit cell:
a: 176.36Å b: 55.34Å c: 46.52Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.203 0.286
Expression system: Escherichia coli

Quick links

Citations

6 review citations

A tale of two pili: assembly and function of pili in bacteria.
Kline et al. (2010)
5 more

3 mentions without citation

Design of Protein Multi-specificity Using an Independent Sequence Search Reduces the Barrier to Low Energy Sequences.
Sevy et al. (2015)
2 more