Mitochondria are highly dynamic double membrane-bound organelles crucial for cellular metabolism, energy conversion, signaling, and apoptosis. They are characterized by extended and intricately folded inner membrane structures termed cristae that were described in the early days of electron microscopy (EM) and later recognized as the main sites of oxidative phosphorylation. Cristae are highly adaptive and variable in shape and size depending on cell type, metabolic state, and developmental stage. Cristae are connected to the mitochondrial inner boundary membrane via crista junctions (CJs). These highly curved tubular openings with a circular or slit-like cross section have been suggested to function as selective pores for proteins and metabolites controlling passageways in and out of the intracristal space. The conserved multisubunit mitochondrial contact site and cristae organizing system (MICOS) localizes to CJs. It is crucial for the formation and stabilization of CJs from yeast to humans and likely plays an important role for the regulation of CJ permeability. MICOS is composed of the Mic60 and Mic10 subcomplexes that both have membrane-shaping activity. Mic60 is anchored in the inner mitochondrial membrane (IMM) via an N-terminal transmembrane (TM) segment and exposes a large domain into the intermembrane space that associates with Mic19. Here you can see the crystal structure of the dimeric mitofilin domain of Mic60 in complex with the CHCH domain of Mic19 (PDB code: 7PV1)
#immolecular ... #molecularart ... #mitochondria ... #cristae ... #junction ... #Mic60 ... #xray
Structure rendered with @proteinimaging and depicted with @corelphotopaint
#immolecular ... #molecularart ... #mitochondria ... #cristae ... #junction ... #Mic60 ... #xray
Structure rendered with @proteinimaging and depicted with @corelphotopaint
