› 4d64

X-ray diffraction
3.2Å resolution

Structure of porin Omp-Pst1 from P. stuartii; the crystallographic symmetry generates a dimer of trimers.

Released:
DOI: 10.2210/pdb4d64/pdb
PDB entry 4d64 coloured by chain, front view.
PDB entry 4d64 coloured by chain, side view.
PDB entry 4d64 coloured by chain, top view.
Source organism: Providencia stuartii
Primary publication:
Porin self-association enables cell-to-cell contact in Providencia stuartii floating communities.
El-Khatib M, Nasrallah C, Lopes J, Tran QT, Tetreau G, Basbous H, Fenel D, Gallet B, Lethier M, Bolla JM, Pagès JM, Vivaudou M, Weik M, Winterhalter M, Colletier JP
Proc Natl Acad Sci U S A 115 E2220-E2228 (2018)
PMID: 29476011

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-122915 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Porin 1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 352 amino acids
Theoretical weight: 39.03 KDa
Source organism: Providencia stuartii
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: E3U904 (Residues: 23-374; Coverage: 94%)
Sequence domains: Gram-negative porin
Structure domains: Porin

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: C2
Unit cell:
a: 151.52Å b: 142.02Å c: 113.32Å
α: 90° β: 131° γ: 90°
R-values:
R R work R free
0.21 0.208 0.261
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

Porins and small-molecule translocation across the outer membrane of Gram-negative bacteria.
Vergalli et al. (2020)
1 more

3 mentions without citation

Porin self-association enables cell-to-cell contact in Providencia stuartii floating communities.
El-Khatib et al. (2018)
2 more