› 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 6d91 coloured by chain and viewed from the front.
PDB 6d91 coloured by chain and viewed from the side.
PDB 6d91 coloured by chain and viewed from the top.
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)
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

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