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-Structure paper
Title | Structural insight into the SAM-mediated assembly of the mitochondrial TOM core complex. |
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Journal, issue, pages | Science, Vol. 373, Issue 6561, Page 1377-1381, Year 2021 |
Publish date | Sep 17, 2021 |
![]() | Qiang Wang / Zeyuan Guan / Liangbo Qi / Jinjin Zhuang / Chen Wang / Sixing Hong / Ling Yan / Yan Wu / Xiaoqian Cao / Jianbo Cao / Junjie Yan / Tingting Zou / Zhu Liu / Delin Zhang / Chuangye Yan / Ping Yin / ![]() |
PubMed Abstract | β barrel outer membrane proteins (β-OMPs) play vital roles in mitochondria, chloroplasts, and Gram-negative bacteria. Evolutionarily conserved complexes such as the mitochondrial sorting and ...β barrel outer membrane proteins (β-OMPs) play vital roles in mitochondria, chloroplasts, and Gram-negative bacteria. Evolutionarily conserved complexes such as the mitochondrial sorting and assembly machinery (SAM) mediate the assembly of β-OMPs. We investigated the SAM-mediated assembly of the translocase of the outer membrane (TOM) core complex. Cryo–electron microscopy structures of SAM–fully folded Tom40 and the SAM-Tom40/Tom5/Tom6 complexes at ~3-angstrom resolution reveal that Sam37 stabilizes the mature Tom40 mainly through electrostatic interactions, thus facilitating subsequent TOM assembly. These results support the β barrel switching model and provide structural insights into the assembly and release of β barrel complexes. |
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Methods | EM (single particle) |
Resolution | 3.01 - 3.05 Å |
Structure data | EMDB-30985, PDB-7e4h: EMDB-30986, PDB-7e4i: |
Source |
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![]() | TRANSLOCASE / yeast / mitochondrial / SAM-Tom40 |