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TitleStructural insight into the SAM-mediated assembly of the mitochondrial TOM core complex.
Journal, issue, pagesScience, Vol. 373, Issue 6561, Page 1377-1381, Year 2021
Publish dateSep 17, 2021
AuthorsQiang 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 Abstractβ 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.
External linksScience / PubMed:34446444
MethodsEM (single particle)
Resolution3.01 - 3.05 Å
Structure data

30985

7e4h

EMDB-30985, PDB-7e4h:
Cryo-EM structure of the yeast mitochondrial SAM-Tom40 complex at 3.0 angstrom
Method: EM (single particle) / Resolution: 3.01 Å

30986

7e4i

EMDB-30986, PDB-7e4i:
Cryo-EM structure of the yeast mitochondrial SAM-Tom40/Tom5/Tom6 complex at 3.0 angstrom
Method: EM (single particle) / Resolution: 3.05 Å

Source
  • saccharomyces cerevisiae s288c (yeast)
KeywordsTRANSLOCASE / yeast / mitochondrial / SAM-Tom40

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