› 4r1i

X-ray diffraction
3.96Å resolution

Structure and Function of Neisseria gonorrhoeae MtrF Illuminates a Class of Antimetabolite Efflux Pumps

Released:
DOI: 10.2210/pdb4r1i/pdb
PDB entry 4r1i coloured by chain, front view.
PDB entry 4r1i coloured by chain, side view.
PDB entry 4r1i coloured by chain, top view.
Source organism: Neisseria gonorrhoeae FA19
Primary publication:
Structure and function of Neisseria gonorrhoeae MtrF illuminates a class of antimetabolite efflux pumps.
Su CC, Bolla JR, Kumar N, Radhakrishnan A, Long F, Delmar JA, Chou TH, Rajashankar KR, Shafer WM, Yu EW
Cell Rep 11 61-70 (2015)
PMID: 25818299

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193216 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative efflux pump component MtrF Chains: A, B
Molecule details ›
Chains: A, B
Length: 522 amino acids
Theoretical weight: 56.17 KDa
Source organism: Neisseria gonorrhoeae FA19
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9RNX2 (Residues: 1-522; Coverage: 100%)
Gene name: mtrF
Sequence domains: AbgT putative transporter family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P65
Unit cell:
a: 120.766Å b: 120.766Å c: 233.897Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.312 0.311 0.338
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Shared Molecular Mechanisms of Membrane Transporters.
Drew et al. (2016)
6 more

8 mentions without citation

Elevator-type mechanisms of membrane transport.
Garaeva et al. (2020)
7 more