转位酶
外膜转位酶
木桶(钟表)
蛋白质靶向
细菌外膜
生物物理学
生物
化学
细胞生物学
膜
膜蛋白
生物化学
材料科学
大肠杆菌
复合材料
染色体易位
基因
作者
Qiang Wang,Zeyuan Guan,Liqun Qi,Jinjin Zhuang,Chen Wang,Sixing Hong,Yan Lv,Yan Wu,Xiaoqian Cao,Jianbo Cao,Junjie Yan,Tingting Zou,Zhu Liu,Delin Zhang,Chuangye Yan,Ping Yin
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:2021-09-17
卷期号:373 (6561): 1377-1381
被引量:18
标识
DOI:10.1126/science.abh0704
摘要
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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