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Structural analysis of a trimeric assembly of the mitochondrial dynamin-like GTPase Mgm1
Structural highlights
FunctionMGM1_YEAST Dynamin-related GTPase required for mitochondrial fusion. Coordinates interaction between the inner and outer mitochondrial membrane to promote the formation of the double membrane.[1] [2] [3] [4] Publication Abstract from PubMedThe fusion of inner mitochondrial membranes requires dynamin-like GTPases, Mgm1 in yeast and OPA1 in mammals, but how they mediate membrane fusion is poorly understood. Here, we determined the crystal structure of Saccharomyces cerevisiae short Mgm1 (s-Mgm1) in complex with GDP. It revealed an N-terminal GTPase (G) domain followed by two helix bundles (HB1 and HB2) and a unique C-terminal lipid-interacting stalk (LIS). Dimers can form through antiparallel HB interactions. Head-to-tail trimers are built by intermolecular interactions between the G domain and HB2-LIS. Biochemical and in vivo analyses support the idea that the assembly interfaces observed here are native and critical for Mgm1 function. We also found that s-Mgm1 interacts with negatively charged lipids via both the G domain and LIS. Based on these observations, we propose that membrane targeting via the G domain and LIS facilitates the in cis assembly of Mgm1, potentially generating a highly curved membrane tip to allow inner membrane fusion. Structural analysis of a trimeric assembly of the mitochondrial dynamin-like GTPase Mgm1.,Yan L, Qi Y, Ricketson D, Li L, Subramanian K, Zhao J, Yu C, Wu L, Sarsam R, Wong M, Lou Z, Rao Z, Nunnari J, Hu J Proc Natl Acad Sci U S A. 2020 Feb 10. pii: 1919116117. doi:, 10.1073/pnas.1919116117. PMID:32041880[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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