8V8T

Asymmetrical subunit from a Drp1 lattice on PA nanotubes

This is a non-PDB format compatible entry.

Summary for 8V8T

• Entry DOI: 10.2210/pdb8v8t/pdb
• EMDB information: 43045
• Descriptor: Dynamin-1-like protein (1 entity in total)
• Functional Keywords: membrane remodeling gtpase, hydrolase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 4
• Total formula weight: 330435.16

Authors

Rochon, K.,Peng, R.,Hutson, A.N.,Stagg, S.M.,Mears, J.A. (deposition date: 2023-12-06, release date: 2025-04-16, Last modification date: 2025-04-30)

Primary citation

Peng, R.,Rochon, K.,Hutson, A.N.,Stagg, S.M.,Mears, J.A.
The Structure of the Drp1 Lattice on Membrane.
J.Mol.Biol., 437:169125-169125, 2025

PubMed Abstract: Mitochondrial health relies on the membrane fission mediated by dynamin-related protein 1 (Drp1). Previous structural studies of Drp1 on remodeled membranes were hampered by heterogeneity, leaving a critical gap in the understanding of the mitochondrial fission mechanisms. Here we present a cryo-electron microscopy structure of full-length human Drp1 decorated on membrane tubules. Using the reconstruction of average subtracted tubular regions (RASTR) technique, we report that Drp1 forms a locally ordered lattice along the tubule without global helical symmetry. The filaments in the lattice are similar to dynamin rungs with conserved stalk interactions. Adjacent filaments are connected by GTPase domain interactions in a novel stacked conformation. We identified two states of the Drp1 lattice among the heterogenous dataset representing conformational changes around hinge 1. Additionally, we observed contact between Drp1 and membrane that can be assigned to the variable domain sequence. Together these structures revealed a putative mechanism by which Drp1 constricts mitochondria membranes in a stepwise, "ratchet" manner.

PubMed: 40185198
DOI: 10.1016/j.jmb.2025.169125

Experimental method

ELECTRON MICROSCOPY (14.73 Å)