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-Structure paper
タイトル | Structure of the intact Tom20 receptor in the human translocase of the outer membrane complex. |
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ジャーナル・号・ページ | PNAS Nexus, Vol. 3, Issue 7, Page pgae269, Year 2024 |
掲載日 | 2024年7月26日 |
![]() | Jiayue Su / Xuyang Tian / Ziyi Wang / Jiawen Yang / Shan Sun / Sen-Fang Sui / ![]() |
PubMed 要旨 | 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 ...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. |
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手法 | EM (単粒子) |
解像度 | 4.72 - 5.92 Å |
構造データ | EMDB-38694, PDB-8xva: ![]() EMDB-60277: TOM core complex ![]() EMDB-60278: whole Tom20 |
由来 |
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![]() | PROTEIN TRANSPORT / mitochondria / transport / membrane protein complex |