4OAI: Crystal Structure Of The Cytosolic Domain Of Mouse Mid51 Dimer Mutant

Citation:
Abstract
Mitochondrial fission requires recruitment of dynamin-related protein 1 (Drp1) to the mitochondrial surface and activation of its GTP-dependent scission function. The Drp1 receptors MiD49 and MiD51 recruit Drp1 to facilitate mitochondrial fission, but their mechanism of action is poorly understood. Using X-ray crystallography, we demonstrate that MiD51 contains a nucleotidyl transferase domain that binds ADP with high affinity. MiD51 recruits Drp1 via a surface loop that functions independently of ADP binding. However, in the absence of nucleotide binding, the recruited Drp1 cannot be activated for fission. Purified MiD51 strongly inhibits Drp1 assembly and GTP hydrolysis in the absence of ADP. Addition of ADP relieves this inhibition and promotes Drp1 assembly into spirals with enhanced GTP hydrolysis. Our results reveal ADP as an essential cofactor for MiD51 during mitochondrial fission.
PDB ID: 4OAIDownload
MMDB ID: 116923
PDB Deposition Date: 2014/1/4
Updated in MMDB: 2014/03
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Similar Structures:
Biological Unit for 4OAI: monomeric; determined by author and by software (PISA)
Molecular Components in 4OAI
Label Count Molecule
Protein (1 molecule)
1
Mitochondrial Dynamic Protein Mid51(Gene symbol: Mief1)
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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