› 3wmg

X-ray diffraction
2.4Å resolution

Crystal structure of an inward-facing eukaryotic ABC multidrug transporter G277V/A278V/A279V mutant in complex with an cyclic peptide inhibitor, aCAP

Released:
DOI: 10.2210/pdb3wmg/pdb
PDB entry 3wmg coloured by chain, front view.
PDB entry 3wmg coloured by chain, side view.
PDB entry 3wmg coloured by chain, top view.
Source organism: Cyanidioschyzon merolae
Primary publication:
Structural basis for gating mechanisms of a eukaryotic P-glycoprotein homolog.
Kodan A, Yamaguchi T, Nakatsu T, Sakiyama K, Hipolito CJ, Fujioka A, Hirokane R, Ikeguchi K, Watanabe B, Hiratake J, Kimura Y, Suga H, Ueda K, Kato H
Proc Natl Acad Sci U S A 111 4049-54 (2014)
PMID: 24591620

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125964 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Probable ATP-dependent transporter ycf16 Chain: A
Molecule details ›
Chain: A
Length: 621 amino acids
Theoretical weight: 67.42 KDa
Source organism: Cyanidioschyzon merolae
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: M1VAN7 (Residues: 93-696; Coverage: 87%)
Gene name: CYME_CMD148C
Sequence domains:
Structure domains:
anti-CmABCB1 peptide Chain: B
Molecule details ›
Chain: B
Length: 19 amino acids
Theoretical weight: 2.11 KDa
Source organism: Cyanidioschyzon merolae
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand DMU 5 x DMU
Ligand TRS 1 x TRS
1 modified residue:
Ligand DTR 1 x DTR

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: R32
Unit cell:
a: 180.49Å b: 180.49Å c: 153.164Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.22 0.219 0.246
Expression systems:
  • Saccharomyces cerevisiae
  • Not provided

Quick links

Citations

28 review citations

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

9 mentions without citation

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