7CK6

Protein translocase of mitochondria

Summary for 7CK6

• Entry DOI: 10.2210/pdb7ck6/pdb
• EMDB information: 30382
• Descriptor: Mitochondrial import receptor subunit TOM40 homolog, Mitochondrial import receptor subunit TOM22 homolog, Mitochondrial import receptor subunit TOM6 homolog, ... (6 entities in total)
• Functional Keywords: complex, mitochondria, structural protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 10
• Total formula weight: 148328.61

Authors

Yang, M.,Wang, W.,Zhang, L.,Chen, X. (deposition date: 2020-07-15, release date: 2020-11-04, Last modification date: 2024-03-27)

Primary citation

Wang, W.,Chen, X.,Zhang, L.,Yi, J.,Ma, Q.,Yin, J.,Zhuo, W.,Gu, J.,Yang, M.
Atomic structure of human TOM core complex.
Cell Discov, 6:67-67, 2020

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 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.

PubMed: 33083003
DOI: 10.1038/s41421-020-00198-2

Experimental method

ELECTRON MICROSCOPY (3.4 Å)