Complex: TOM40 mitochondrial outer membrane translocase holocomplex
Macromolecular complex annotations are imported from the Complex Portal. These annotations have been derived from physical molecular interaction evidence extracted from the literature and cross-referenced in the entry, or by curator inference from information on homologs in closely related species or by inference from scientific background.
- Curated by
- IntAct
- ComplexAc
- CPX-474
- Systematic Name
- TOM5:TOM6:TOM7:TOM20:TOM22:TOM40:TOM70
- SGD ID
- SGD:S000218019
- Aliases
- Mitochondrial outer membrane translocase holocomplex ; Preprotein translocase of the outer mitochondrial membrane ; TOM holocomplex
- Description
- Translocase in the outer mitochondrial membrane that mediates the import of precursor protein and mediates inset of some resident outer membrane proteins. Most mitochondrial proteins are synthesized in the cytosol, imported into mitochondria, sorted to one of the four submitochondrial compartments, where they function, and attain their functional native conformation, which is often facilitated by assembly into the membrane or a multiprotein complex. The holo TOM complex contains two or three pores, each of which has a diameter of approximately 20A. When translocation by the TOM complex is coupled with that by the TIM23 or TIM22 complex, the TOM channel can operate as a passive pore to allow passage of the polypeptide segment, which is `pulled' by the TIM complex with the aid of differenial membrane potential and/or ATP. When translocation is uncoupled from the inner-membrane translocators, the TOM complex uses both the stop-transfer pathway, which consists of two steps, the first requiring a membrane potential and an ATP-dependent chaperone mHsp70, and a second mechanism involving the folding of an N-terminal domain that has already crossed the outer membrane and can function as a trap in the intermembrane space to drive translocation of the C-terminal part of the protein by a Brownian ratchet mechanism.
Complex Diagram
This diagram displays the protein subunits (blue) of the complex and how they interact with each other. Interactions with other relevant participants such as small molecules (purple), sub-complexes (yellow), and other subunits (red) are also shown. If a participant appears in the diagram with no lines connected to it, then its specific interactions with other participants are currently unknown.
Subunits
This table lists all participants of the complex (proteins, small molecules, nucleic acids, etc.) and their respective stoichiometry. A brief description is also provided for each participant in the table.
Increase the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through its pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table.
| Subunit | Description | Stoichiometry |
|---|
Gene Ontology
Gene Ontology (GO) terms that describe the function of a complex, the biological process in which it participates, or its cellular location. Click on a term for its definition and other objects annotated to that term.
- Biological Process
-
- involved in protein insertion into mitochondrial outer membrane (IDA)
- Cellular Component
-
- located in mitochondrial outer membrane (IDA)
Shared Annotations
This diagram displays Gene Ontology terms (green) and subunits (blue) that are shared between the given macromolecular complex (black) and other yeast complexes (yellow). The shared GO terms or subunits can be visualized separately using the radio button at the bottom of the graph. Note: No diagram is shown ("No shared annotations") if there are less than 2 shared annotations (either GO terms or subunits of other complexes) between this complex and any other complexes.
References
List of references used specifically to curate the information on this page.
- Araiso Y, et al. (2019) Structure of the mitochondrial import gate reveals distinct preprotein paths. Nature 575(7782):395-401 PMID: 31600774
- Tucker K and Park E (2019) Cryo-EM structure of the mitochondrial protein-import channel TOM complex at near-atomic resolution. Nat Struct Mol Biol 26(12):1158-1166 PMID: 31740857
- Endo T, et al. (2003) Functional cooperation and separation of translocators in protein import into mitochondria, the double-membrane bounded organelles. J Cell Sci 116(Pt 16):3259-67 PMID: 12857785
Resources
IntAct | ModelArchive | PDB:6UCU | PDB:6UCV ... Show all Show fewer