title: Structure and function of mitochondrial supercomplexes.
abstract: The five complexes (complexes I-V) of the oxidative phosphorylation (OXPHOS) system of mitochondria can be extracted in the form of active supercomplexes. Single-particle electron microscopy has provided 2D and 3D data describing the interaction between complexes I and III, among I, III and IV and in a dimeric form of complex V, between two ATP synthase monomers. The stable interactions are called supercomplexes which also form higher-ordered oligomers. Cryo-electron tomography provides new insights on how these supercomplexes are arranged within intact mitochondria. The structure and function of OXPHOS supercomplexes are discussed.
authors.affiliation: Electron microscopy group, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.
authors.forename: Natalya V
authors.initials: NV
authors.lastname: Dudkina
authors.forename: Roman
authors.initials: R
authors.lastname: Kouril
authors.forename: Katrin
authors.initials: K
authors.lastname: Peters
authors.forename: Hans-Peter
authors.initials: HP
authors.lastname: Braun
authors.forename: Egbert J
authors.initials: EJ
authors.lastname: Boekema
mesh_terms: D000460:Chlorophyta / Q000378:metabolism; D055032:Electron Microscope Tomography; D045222:Electron Transport Chain Complex Proteins / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D021621:Imaging, Three-Dimensional; D008854:Microscopy, Electron; D008928:Mitochondria / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D008958:Models, Molecular; D010085:Oxidative Phosphorylation; D010940:Plant Proteins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D055503:Protein Multimerization
chemical_list: D045222:Electron Transport Chain Complex Proteins; D010940:Plant Proteins