› 2qh7

X-ray diffraction
1.5Å resolution

MitoNEET is a uniquely folded 2Fe-2S outer mitochondrial membrane protein stabilized by pioglitazone

Released:
DOI: 10.2210/pdb2qh7/pdb
PDB entry 2qh7 coloured by chain, front view.
PDB entry 2qh7 coloured by chain, side view.
PDB entry 2qh7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
MitoNEET is a uniquely folded 2Fe 2S outer mitochondrial membrane protein stabilized by pioglitazone.
Paddock ML, Wiley SE, Axelrod HL, Cohen AE, Roy M, Abresch EC, Capraro D, Murphy AN, Nechushtai R, Dixon JE, Jennings PA
Proc Natl Acad Sci U S A 104 14342-7 (2007)
PMID: 17766440

Function and Biology Details

Reaction catalysed: 
L-cysteine + 2-oxoglutarate = 2-oxo-3-sulfanylpropanoate + L-glutamate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192731 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CDGSH iron-sulfur domain-containing protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 76 amino acids
Theoretical weight: 8.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NZ45 (Residues: 33-108; Coverage: 70%)
Gene names: C10orf70, CISD1, MDS029, ZCD1
Sequence domains: Iron-binding zinc finger CDGSH type
Structure domains: CDGSH iron-sulfur domain, mitoNEET-type

Ligands and Environments

1 bound ligand:
Ligand FES 2 x FES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1, SSRL BEAMLINE BL9-2
Spacegroup: P212121
Unit cell:
a: 46.806Å b: 49.621Å c: 59.006Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.182 0.223
Expression system: Escherichia coli

Quick links

Citations

34 review citations

Neuroprotective strategies involving ROS in Alzheimer disease.
Dumont et al. (2011)
33 more

34 mentions without citation

Advanced paramagnetic resonance spectroscopies of iron-sulfur proteins: Electron nuclear double resonance (ENDOR) and electron spin echo envelope modulation (ESEEM).
Cutsail et al. (2015)
33 more