Abstract
OPA1 is a dynamin-related GTPase that controls mitochondrial fusion, cristae remodeling, energetics and mtDNA maintenance. However, the molecular architecture of OPA1 is poorly understood. Here we modeled the structure of human OPA1 by the threading approach. We found that the C-terminal region of the OPA1 protein had multiple functional domains, while the N-terminal region was rich in alpha helices and did not include specific domains. For the short soluble forms of OPA1, we observed that there were obvious hydrophobic regions near the two cleavage sites and the N-terminal was positively charged after cleavage. The blue native analysis revealed that the protein could form stable homodimers. In addition, the evolutionary conservation of the C-terminal region, where most of the known mutated disease-related sites were located, was significantly higher than that of the N-terminal region. These findings provided new insights into the structure and biochemical function of OPA1.