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TitleStructure of the intact Tom20 receptor in the human translocase of the outer membrane complex.
Journal, issue, pagesPNAS Nexus, Vol. 3, Issue 7, Page pgae269, Year 2024
Publish dateJul 26, 2024
AuthorsJiayue Su / Xuyang Tian / Ziyi Wang / Jiawen Yang / Shan Sun / Sen-Fang Sui /
PubMed AbstractThe translocase of the outer membrane (TOM) complex serves as the main gate for preproteins entering mitochondria and thus plays a pivotal role in sustaining mitochondrial stability. Precursor ...The translocase of the outer membrane (TOM) complex serves as the main gate for preproteins entering mitochondria and thus plays a pivotal role in sustaining mitochondrial stability. Precursor proteins, featuring amino-terminal targeting signals (presequences) or internal targeting signals, are recognized by the TOM complex receptors Tom20, Tom22, and Tom70, and then translocated into mitochondria through Tom40. By using chemical cross-linking to stabilize Tom20 in the TOM complex, this study unveils the structure of the human TOM holo complex, encompassing the intact Tom20 component, at a resolution of approximately 6 Å by cryo-electron microscopy. Our structure shows the TOM holo complex containing only one Tom20 subunit, which is located right at the center of the complex and stabilized by extensive interactions with Tom22, Tom40, and Tom6. Based on the structure, we proposed a possible translocation mode of TOM complex, by which different receptors could work simultaneously to ensure that the preproteins recognized by them are all efficiently translocated into the mitochondria.
External linksPNAS Nexus / PubMed:39071881 / PubMed Central
MethodsEM (single particle)
Resolution4.72 - 5.92 Å
Structure data

38694

8xva

EMDB-38694, PDB-8xva:
Human TOM complex with whole Tom20
Method: EM (single particle) / Resolution: 5.92 Å

EMDB-60277: TOM core complex
Method: EM (single particle) / Resolution: 5.62 Å

EMDB-60278: whole Tom20
Method: EM (single particle) / Resolution: 4.72 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN TRANSPORT / mitochondria / transport / membrane protein complex

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