› 4oaf

X-ray diffraction
2.2Å resolution

Crystal structure of the cytosolic domain of mouse MiD51

Released:
DOI: 10.2210/pdb4oaf/pdb
PDB entry 4oaf coloured by chain, front view.
PDB entry 4oaf coloured by chain, side view.
PDB entry 4oaf coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
The mitochondrial fission receptor MiD51 requires ADP as a cofactor.
Losón OC, Liu R, Rome ME, Meng S, Kaiser JT, Shan SO, Chan DC
Structure 22 367-77 (2014)
PMID: 24508339

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183866 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mitochondrial dynamics protein MID51 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 335 amino acids
Theoretical weight: 37.25 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8BGV8 (Residues: 134-463; Coverage: 71%)
Gene names: Mid51, Mief1, Smcr7l
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P21
Unit cell:
a: 91.075Å b: 78.592Å c: 102.31Å
α: 90° β: 96.61° γ: 90°
R-values:
R R work R free
0.205 0.204 0.258
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

30 review citations

Metabolic regulation of mitochondrial dynamics.
Mishra et al. (2016)
29 more

4 mentions without citation

The mitochondrial fission receptor MiD51 requires ADP as a cofactor.
Losón et al. (2014)
3 more