› 5n9i

X-ray diffraction
1.91Å resolution

STRUCTURE OF 206-GVVTSE-211, THE STERIC ZIPPER THAT SUPPORTS THE SELF-ASSOCIATION OF P. STUARTII OMP-PST1 INTO DIMERS OF TRIMERS

Released:
DOI: 10.2210/pdb5n9i/pdb
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PDB entry 5n9i coloured by chain, front view.
PDB entry 5n9i coloured by chain, side view.
PDB entry 5n9i 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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-122916 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Porin 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 6 amino acids
Theoretical weight: 591 Da
Source organism: Providencia stuartii
Expression system: Not provided
UniProt:
  • Canonical: E3U904 (Residues: 228-233; Coverage: 2%)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P1
Unit cell:
a: 4.8Å b: 16.91Å c: 45.45Å
α: 90.05° β: 90.01° γ: 90.05°
R-values:
R R work R free
0.157 0.147 0.206
Expression system: Not provided

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Citations

2 review citations

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

1 mention without citation

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

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