4BEJ

Nucleotide-free Dynamin 1-like protein (DNM1L, DRP1, DLP1)

Summary for 4BEJ

• Entry DOI: 10.2210/pdb4bej/pdb
• Descriptor: DYNAMIN 1-LIKE PROTEIN (1 entity in total)
• Functional Keywords: hydrolase, g protein, mitochondrial fission, membrane remodeling, apoptosis
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm, cytosol: O00429
• Total number of polymer chains: 4
• Total formula weight: 276842.06

Authors

Froehlich, C.,Schwefel, D.,Faelber, K.,Daumke, O. (deposition date: 2013-03-11, release date: 2013-04-24, Last modification date: 2023-12-20)

Primary citation

Frohlich, C.,Grabiger, S.,Schwefel, D.,Faelber, K.,Rosenbaum, E.,Mears, J.,Rocks, O.,Daumke, O.
Structural Insights Into Oligomerization and Mitochondrial Remodelling of Dynamin 1-Like Protein.
Embo J., 32:1280-, 2013

PubMed Abstract: Dynamin 1-like protein (DNM1L) mediates fission of mitochondria and peroxisomes, and dysfunction of DNM1L has been implicated in several neurological disorders. To study the molecular basis of mitochondrial remodelling, we determined the crystal structure of DNM1L that is comprised of a G domain, a bundle signalling element and a stalk. DNM1L assembled via a central stalk interface, and mutations in this interface disrupted dimerization and interfered with membrane binding and mitochondrial targeting. Two sequence stretches at the tip of the stalk were shown to be required for ordered assembly of DNM1L on membranes and its function in mitochondrial fission. In the crystals, DNM1L dimers further assembled via a second, previously undescribed, stalk interface to form a linear filament. Mutations in this interface interfered with liposome tubulation and mitochondrial remodelling. Based on these results and electron microscopy reconstructions, we propose an oligomerization mode for DNM1L which differs from that of dynamin and might be adapted to the remodelling of mitochondria.

PubMed: 23584531
DOI: 10.1038/EMBOJ.2013.74

Experimental method

X-RAY DIFFRACTION (3.483 Å)