1T3J
Mitofusin domain HR2 V686M/I708M mutant
Summary for 1T3J
| Entry DOI | 10.2210/pdb1t3j/pdb |
| Descriptor | mitofusin 1 (2 entities in total) |
| Functional Keywords | coiled coil antiparallel, dimer, membrane protein |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Mitochondrion outer membrane; Multi-pass membrane protein (By similarity): Q811U4 |
| Total number of polymer chains | 1 |
| Total formula weight | 11107.45 |
| Authors | Koshiba, T.,Detmer, S.A.,Kaiser, J.T.,Chen, H.,McCaffery, J.M.,Chan, D.C. (deposition date: 2004-04-26, release date: 2004-08-17, Last modification date: 2024-02-14) |
| Primary citation | Koshiba, T.,Detmer, S.A.,Kaiser, J.T.,Chen, H.,McCaffery, J.M.,Chan, D.C. Structural basis of mitochondrial tethering by mitofusin complexes Science, 305:858-862, 2004 Cited by PubMed Abstract: Vesicle fusion involves vesicle tethering, docking, and membrane merger. We show that mitofusin, an integral mitochondrial membrane protein, is required on adjacent mitochondria to mediate fusion, which indicates that mitofusin complexes act in trans (that is, between adjacent mitochondria). A heptad repeat region (HR2) mediates mitofusin oligomerization by assembling a dimeric, antiparallel coiled coil. The transmembrane segments are located at opposite ends of the 95 angstrom coiled coil and provide a mechanism for organelle tethering. Consistent with this proposal, truncated mitofusin, in an HR2-dependent manner, causes mitochondria to become apposed with a uniform gap. Our results suggest that HR2 functions as a mitochondrial tether before fusion. PubMed: 15297672DOI: 10.1126/science.1099793 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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