› 4pl0

X-ray diffraction
2.7Å resolution

Crystal structure of the antibacterial peptide ABC transporter McjD in an outward occluded state

Released:
DOI: 10.2210/pdb4pl0/pdb
PDB entry 4pl0 coloured by chain, front view.
PDB entry 4pl0 coloured by chain, side view.
PDB entry 4pl0 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure of an antibacterial peptide ATP-binding cassette transporter in a novel outward occluded state.
Choudhury HG, Tong Z, Mathavan I, Li Y, Iwata S, Zirah S, Rebuffat S, van Veen HW, Beis K
Proc Natl Acad Sci U S A 111 9145-50 (2014)
PMID: 24920594

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 580 amino acids
Theoretical weight: 65.48 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: Q9X2W0 (Residues: 1-580; Coverage: 100%)
Gene name: mcjD
Sequence domains:
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

3 bound ligands:
Ligand ANP 2 x ANP
Ligand MG 2 x MG
Ligand BNG 2 x BNG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 80.83Å b: 107.92Å c: 232.96Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.248 0.247 0.266
Expression system: Escherichia coli K-12

Quick links

Citations

29 review citations

Mechanistic diversity in ATP-binding cassette (ABC) transporters.
Locher KP. (2016)
28 more

16 mentions without citation

Structural and functional diversity calls for a new classification of ABC transporters.
Thomas et al. (2020)
15 more