8UY3
Fem1B with FNIP1 and Tom20 fragment
Summary for 8UY3
| Entry DOI | 10.2210/pdb8uy3/pdb |
| Descriptor | Protein fem-1 homolog B, Folliculin-interacting protein 1, Mitochondrial import receptor subunit TOM20 homolog, ... (7 entities in total) |
| Functional Keywords | fem1b fnp1 ubiquitin, proteasome, reductive stress response, tom complex electron transport chain mitochondria, protein binding |
| Biological source | Mus musculus (house mouse) More |
| Total number of polymer chains | 11 |
| Total formula weight | 206610.99 |
| Authors | Gee, C.L.,Manford, A.G.,McMinimy, R.,Rape, M. (deposition date: 2023-11-12, release date: 2025-03-19) |
| Primary citation | McMinimy, R.,Manford, A.G.,Gee, C.L.,Chandrasekhar, S.,Mousa, G.A.,Chuang, J.,Phu, L.,Shih, K.Y.,Rose, C.M.,Kuriyan, J.,Bingol, B.,Rape, M. Reactive oxygen species control protein degradation at the mitochondrial import gate. Mol.Cell, 84:4612-4628.e13, 2024 Cited by PubMed Abstract: While reactive oxygen species (ROS) have long been known to drive aging and neurodegeneration, their persistent depletion below basal levels also disrupts organismal function. Cells counteract loss of basal ROS via the reductive stress response, but the identity and biochemical activity of ROS sensed by this pathway remain unknown. Here, we show that the central enzyme of the reductive stress response, the E3 ligase Cullin 2-FEM1 homolog B (CUL2), specifically acts at mitochondrial TOM complexes, where it senses ROS produced by complex III of the electron transport chain (ETC). ROS depletion during times of low ETC activity triggers the localized degradation of CUL2 substrates, which sustains mitochondrial import and ensures the biogenesis of the rate-limiting ETC complex IV. As complex III yields most ROS when the ETC outpaces metabolic demands or oxygen availability, basal ROS are sentinels of mitochondrial activity that help cells adjust their ETC to changing environments, as required for cell differentiation and survival. PubMed: 39642856DOI: 10.1016/j.molcel.2024.11.004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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