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-Structure paper
Title | Atomic structure of human TOM core complex. |
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Journal, issue, pages | Cell Discov, Vol. 6, Page 67, Year 2020 |
Publish date | Sep 29, 2020 |
Authors | Wenhe Wang / Xudong Chen / Laixing Zhang / Jingbo Yi / Qingxi Ma / Jian Yin / Wei Zhuo / Jinke Gu / Maojun Yang / |
PubMed Abstract | The translocase of the outer mitochondrial membrane (TOM) complex is the main entry gate for mitochondrial precursor proteins synthesized on cytosolic ribosomes. Here we report the single-particle ...The translocase of the outer mitochondrial membrane (TOM) complex is the main entry gate for mitochondrial precursor proteins synthesized on cytosolic ribosomes. Here we report the single-particle cryo-electron microscopy (cryo-EM) structure of the dimeric human TOM core complex (TOM-CC). Two Tom40 β-barrel proteins, connected by two Tom22 receptor subunits and one phospholipid, form the protein-conducting channels. The small Tom proteins Tom5, Tom6, and Tom7 surround the channel and have notable configurations. The distinct electrostatic features of the complex, including the pronounced negative interior and the positive regions at the periphery and center of the dimer on the intermembrane space (IMS) side, provide insight into the preprotein translocation mechanism. Further, two dimeric TOM complexes may associate to form tetramer in the shape of a parallelogram, offering a potential explanation into the unusual structural features of Tom subunits and a new perspective of viewing the import of mitochondrial proteins. |
External links | Cell Discov / PubMed:33083003 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.4 Å |
Structure data | EMDB-30382, PDB-7ck6: |
Chemicals | ChemComp-PC1: |
Source |
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Keywords | STRUCTURAL PROTEIN / Complex / Mitochondria |