| Structural highlights
Function
SAM50_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 PubMed
beta 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
- ↑ Kozjak V, Wiedemann N, Milenkovic D, Lohaus C, Meyer HE, Guiard B, Meisinger C, Pfanner N. An essential role of Sam50 in the protein sorting and assembly machinery of the mitochondrial outer membrane. J Biol Chem. 2003 Dec 5;278(49):48520-3. PMID:14570913 doi:10.1074/jbc.C300442200
- ↑ 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. Structural insight into the SAM-mediated assembly of the mitochondrial TOM core complex. Science. 2021 Sep 17;373(6561):1377-1381. PMID:34446444 doi:10.1126/science.abh0704
|
