6UCU
Cryo-EM structure of the mitochondrial TOM complex from yeast (dimer)
Summary for 6UCU
| Entry DOI | 10.2210/pdb6ucu/pdb |
| EMDB information | 20728 20729 |
| Descriptor | Mitochondrial import receptor subunit TOM40, Mitochondrial import receptor subunit TOM22, Mitochondrial import receptor subunit TOM5, ... (6 entities in total) |
| Functional Keywords | membrane protein, mitochondrial protein import, mitochondrial outer membrane, protein translocation, translocase |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Total number of polymer chains | 10 |
| Total formula weight | 191695.65 |
| Authors | Park, E.,Tucker, K. (deposition date: 2019-09-17, release date: 2019-11-06, Last modification date: 2024-03-20) |
| Primary citation | Tucker, K.,Park, E. Cryo-EM structure of the mitochondrial protein-import channel TOM complex at near-atomic resolution. Nat.Struct.Mol.Biol., 26:1158-1166, 2019 Cited by PubMed Abstract: Nearly all mitochondrial proteins are encoded by the nuclear genome and imported into mitochondria after synthesis on cytosolic ribosomes. These precursor proteins are translocated into mitochondria by the TOM complex, a protein-conducting channel in the mitochondrial outer membrane. We have determined high-resolution cryo-EM structures of the core TOM complex from Saccharomyces cerevisiae in dimeric and tetrameric forms. Dimeric TOM consists of two copies each of five proteins arranged in two-fold symmetry: pore-forming β-barrel protein Tom40 and four auxiliary α-helical transmembrane proteins. The pore of each Tom40 has an overall negatively charged inner surface attributed to multiple functionally important acidic patches. The tetrameric complex is essentially a dimer of dimeric TOM, which may be capable of forming higher-order oligomers. Our study reveals the detailed molecular organization of the TOM complex and provides new insights about the mechanism of protein translocation into mitochondria. PubMed: 31740857DOI: 10.1038/s41594-019-0339-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.06 Å) |
Structure validation
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