6FGZ
Cyanidioschyzon merolae Dnm1 (CmDnm1)
Summary for 6FGZ
| Entry DOI | 10.2210/pdb6fgz/pdb |
| Descriptor | Dynamin (1 entity in total) |
| Functional Keywords | dynamin, mitochondrial fission, lipid binding protein |
| Biological source | Cyanidioschyzon merolae (Red alga) |
| Total number of polymer chains | 1 |
| Total formula weight | 87294.98 |
| Authors | Bohuszewicz, O.,Low, H.H. (deposition date: 2018-01-11, release date: 2018-08-15, Last modification date: 2024-01-17) |
| Primary citation | Bohuszewicz, O.,Low, H.H. Structure of a mitochondrial fission dynamin in the closed conformation. Nat. Struct. Mol. Biol., 25:722-731, 2018 Cited by PubMed Abstract: Dynamin 1-like proteins (DNM1-L) are mechanochemical GTPases that induce membrane fission in mitochondria and peroxisomes. Their mechanism depends on conformational changes driven by nucleotide and lipid cycling. Here we show the crystal structure of a mitochondrial fission dynamin (CmDnm1) from the algae Cyanidioschyzon merolae. Unlike other eukaryotic dynamin structures, CmDnm1 is in a hinge 1 closed conformation, with the GTPase domain compacted against the stalk. Within the crystal, CmDnm1 packs as a diamond-shaped tetramer that is consistent with an inactive off-membrane state. Crosslinking, photoinduced electron transfer assays, and electron microscopy verify these structures. In vitro, CmDnm1 forms concentration-dependent rings and protein-lipid tubes reminiscent of DNM1-L and classical dynamin with hinge 1 open. Our data provides a mechanism for filament collapse and membrane release that may extend to other dynamin family members. Additionally, hinge 1 closing may represent a key conformational change that contributes to membrane fission. PubMed: 30061604DOI: 10.1038/s41594-018-0097-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (7.002 Å) |
Structure validation
Download full validation report
