› 6d91

X-ray diffraction
2.36Å resolution

Crystal structure of the Deinococcus radiodurans Nramp/MntH divalent transition metal transporter in the outward-open, apo conformation

Released:
DOI: 10.2210/pdb6d91/pdb
PDB entry 6d91 coloured by chain, front view.
PDB entry 6d91 coloured by chain, side view.
PDB entry 6d91 coloured by chain, top view.
Source organism: Deinococcus radiodurans R1
Primary publication:
Structures in multiple conformations reveal distinct transition metal and proton pathways in an Nramp transporter.
Bozzi AT, Zimanyi CM, Nicoludis JM, Lee BK, Zhang CH, Gaudet R
Elife 8 (2019)
PMID: 30714568

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-193268 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Divalent metal cation transporter MntH Chain: A
Molecule details ›
Chain: A
Length: 412 amino acids
Theoretical weight: 44.61 KDa
Source organism: Deinococcus radiodurans R1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9RTP8 (Residues: 35-436; Coverage: 92%)
Gene names: DR_1709, mntH
Sequence domains: Natural resistance-associated macrophage protein-like

Ligands and Environments

1 bound ligand:
Ligand OLC 6 x OLC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: C2
Unit cell:
a: 101.919Å b: 75.508Å c: 53.151Å
α: 90° β: 98.07° γ: 90°
R-values:
R R work R free
0.249 0.244 0.299
Expression system: Escherichia coli

Quick links

Citations

3 review citations

General principles of secondary active transporter function.
Beckstein et al. (2022)
2 more

5 mentions without citation

Molecular Mechanism of Nramp-Family Transition Metal Transport.
Bozzi et al. (2021)
4 more