› 4aui

X-ray diffraction
3.2Å resolution

STRUCTURE AND FUNCTION OF THE PORB PORIN FROM DISSEMINATING N. GONORRHOEAE

Released:
DOI: 10.2210/pdb4aui/pdb
PDB entry 4aui coloured by chain, front view.
PDB entry 4aui coloured by chain, side view.
PDB entry 4aui coloured by chain, top view.
Source organism: Neisseria gonorrhoeae
Primary publication:
Structure and function of the PorB porin from disseminating Neisseria gonorrhoeae.
Zeth K, Kozjak-Pavlovic V, Faulstich M, Fraunholz M, Hurwitz R, Kepp O, Rudel T
Biochem J 449 631-42 (2013)
PMID: 23095086

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo trimer (preferred)
monomeric
Assembly name:
PDBe Complex ID:
PDB-CPX-175907 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Porin (PorB) Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 327 amino acids
Theoretical weight: 35.85 KDa
Source organism: Neisseria gonorrhoeae
UniProt:
  • Canonical: Q51056 (Residues: 1-327; Coverage: 100%)
Gene name: porB
Sequence domains: Gram-negative porin
Structure domains: Porin
POLY ALA Chains: D, E, F
Molecule details ›
Chains: D, E, F
Length: 8 amino acids
Theoretical weight: 587 Da
Source organism: Neisseria gonorrhoeae

Ligands and Environments

3 bound ligands:
Ligand ATP 3 x ATP
Ligand PO4 6 x PO4
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: C2
Unit cell:
a: 114.05Å b: 111.47Å c: 88.34Å
α: 90° β: 102.07° γ: 90°
R-values:
R R work R free
0.224 0.221 0.268

Quick links

Citations

3 review citations

Fluoroquinolone resistance: mechanisms, impact on bacteria, and role in evolutionary success.
Redgrave et al. (2014)
2 more

7 mentions without citation

Crystallographic analysis of Neisseria meningitidis PorB extracellular loops potentially implicated in TLR2 recognition.
Kattner et al. (2014)
6 more