› 5ofp

X-ray diffraction
4.71Å resolution

Structure of the antibacterial peptide ABC transporter McjD in an apo inward occluded conformation

Released:
DOI: 10.2210/pdb5ofp/pdb
PDB entry 5ofp coloured by chain, front view.
PDB entry 5ofp coloured by chain, side view.
PDB entry 5ofp coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural basis for antibacterial peptide self-immunity by the bacterial ABC transporter McjD.
Bountra K, Hagelueken G, Choudhury HG, Corradi V, El Omari K, Wagner A, Mathavan I, Zirah S, Yuan Wahlgren W, Tieleman DP, Schiemann O, Rebuffat S, Beis K
EMBO J 36 3062-3079 (2017)
PMID: 28864543

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194904 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Microcin-J25 export ATP-binding/permease protein McjD Chain: A
Molecule details ›
Chain: A
Length: 580 amino acids
Theoretical weight: 65.48 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli str. K-12 substr. MG1655
UniProt:
  • Canonical: Q9X2W0 (Residues: 1-580; Coverage: 100%)
Gene name: mcjD
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P4222
Unit cell:
a: 87.85Å b: 87.85Å c: 351.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.314 0.313 0.334
Expression system: Escherichia coli str. K-12 substr. MG1655

Quick links

Citations

14 review citations

Multidrug efflux pumps: structure, function and regulation.
Du et al. (2018)
13 more

4 mentions without citation

Mechanics and pharmacology of substrate selection and transport by eukaryotic ABC exporters.
Srikant et al. (2019)
3 more