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| Item Type: | Preprint |
|---|---|
| Title: | Integrative modelling reveals the structure of the human Mic60-Mic19 subcomplex and its role as a diffusion barrier in mitochondria |
| Creators Name: | Nathanail, Evangelia, Rolando, Edoardo, Ruwolt, Max, Zaporozhets, Iryna, Liu, Fan, Clementi, Cecilia and Daumke, Oliver |
| Abstract: | Mitochondrial crista junctions (CJs) operate as regulated gateways into the cristae microenvironment, whose protein, metabolite, and ion compositions are finely tuned for mitochondrial function. The Mic60-Mic19 complex of the mitochondrial contact site and cristae organizing system (MICOS) complex was suggested to span across CJs and act as a diffusion barrier, but little is known of how its dynamic architecture facilitates this task. To address this open question, we determined the crystal structure of an amino-terminal dimeric helical bundle of human Mic60. These and previous structural and biochemical data were harnessed in molecular dynamic (MD) simulations to develop a dynamic model of the human tetrameric Mic60-Mic19 subcomplex in the CJ environment, to validate its architecture using in organello cross-linking data and to computationally characterize its function as a diffusion barrier. Our integrative structural biology approach enables the functional investigation of flexible, multidomain protein complexes which escape conventional structural biology methods. |
| Source: | bioRxiv |
| Publisher: | Cold Spring Harbor Laboratory Press |
| Article Number: | 2026.01.30.702776 |
| Date: | 30 January 2026 |
| Official Publication: | https://doi.org/10.64898/2026.01.30.702776 |
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