› 3mkt

X-ray diffraction
3.65Å resolution

Structure of a Cation-bound Multidrug and Toxin Compound Extrusion (MATE) transporter

Released:
DOI: 10.2210/pdb3mkt/pdb
PDB entry 3mkt coloured by chain, front view.
PDB entry 3mkt coloured by chain, side view.
PDB entry 3mkt coloured by chain, top view.
Source organism: Vibrio cholerae O1 biovar El Tor str. N16961
Primary publication:
Structure of a cation-bound multidrug and toxic compound extrusion transporter.
He X, Szewczyk P, Karyakin A, Evin M, Hong WX, Zhang Q, Chang G
Nature 467 991-4 (2010)
PMID: 20861838

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163787 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Multi antimicrobial extrusion protein (Na(+)/drug antiporter) MATE-like MDR efflux pump Chains: A, B
Molecule details ›
Chains: A, B
Length: 460 amino acids
Theoretical weight: 49.76 KDa
Source organism: Vibrio cholerae O1 biovar El Tor str. N16961
Expression system: Escherichia coli

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P21212
Unit cell:
a: 140.84Å b: 238.77Å c: 45.31Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.312 0.312 0.343
Expression system: Escherichia coli

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Citations

46 review citations

The challenge of efflux-mediated antibiotic resistance in Gram-negative bacteria.
Li et al. (2015)
45 more

27 mentions without citation

Glycines: role in α-helical membrane protein structures and a potential indicator of native conformation.
Dong et al. (2012)
26 more