Structural highlights
FunctionSAM50_YEAST Component of the mitochondrial outer membrane sorting assembly machinery (SAM or TOB) complex, which is required for the sorting of proteins with complicated topology, such as beta-barrel proteins, to the mitochondrial outer membrane after import by the TOM complex.[1] Publication Abstract from PubMedbeta barrel outer membrane proteins (beta-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 beta-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 beta barrel switching model and provide structural insights into the assembly and release of beta barrel complexes. Structural insight into the SAM-mediated assembly of the mitochondrial TOM core complex.,Wang Q, Guan Z, Qi L, Zhuang J, Wang C, Hong S, Yan L, Wu Y, Cao X, Cao J, Yan J, Zou T, Liu Z, Zhang D, Yan C, Yin P Science. 2021 Sep 17;373(6561):1377-1381. doi: 10.1126/science.abh0704. Epub 2021 , Aug 26. PMID:34446444[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||
This page was last modified 05:43, 5 June 2024.