5WP9
Structural Basis of Mitochondrial Receptor Binding and Constriction by Dynamin-Related Protein 1
This is a non-PDB format compatible entry.
Summary for 5WP9
| Entry DOI | 10.2210/pdb5wp9/pdb |
| EMDB information | 8874 |
| Descriptor | Dynamin-1-like protein, Mitochondrial dynamics protein MID49, PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER, ... (4 entities in total) |
| Functional Keywords | mitochondrial division, dynamin related-protein-1, nucleotide, mid49, protein fibril |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 16 |
| Total formula weight | 929988.29 |
| Authors | Kalia, R.,Wang, R.Y.R.,Yusuf, A.,Thomas, P.V.,Agard, D.A.,Shaw, J.M.,Frost, A. (deposition date: 2017-08-03, release date: 2018-06-20, Last modification date: 2024-03-13) |
| Primary citation | Kalia, R.,Wang, R.Y.,Yusuf, A.,Thomas, P.V.,Agard, D.A.,Shaw, J.M.,Frost, A. Structural basis of mitochondrial receptor binding and constriction by DRP1. Nature, 558:401-405, 2018 Cited by PubMed Abstract: Mitochondrial inheritance, genome maintenance and metabolic adaptation depend on organelle fission by dynamin-related protein 1 (DRP1) and its mitochondrial receptors. DRP1 receptors include the paralogues mitochondrial dynamics proteins of 49 and 51 kDa (MID49 and MID51) and mitochondrial fission factor (MFF); however, the mechanisms by which these proteins recruit and regulate DRP1 are unknown. Here we present a cryo-electron microscopy structure of full-length human DRP1 co-assembled with MID49 and an analysis of structure- and disease-based mutations. We report that GTP induces a marked elongation and rotation of the GTPase domain, bundle-signalling element and connecting hinge loops of DRP1. In this conformation, a network of multivalent interactions promotes the polymerization of a linear DRP1 filament with MID49 or MID51. After co-assembly, GTP hydrolysis and exchange lead to MID receptor dissociation, filament shortening and curling of DRP1 oligomers into constricted and closed rings. Together, these views of full-length, receptor- and nucleotide-bound conformations reveal how DRP1 performs mechanical work through nucleotide-driven allostery. PubMed: 29899447DOI: 10.1038/s41586-018-0211-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.22 Å) |
Structure validation
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