7E4I
Cryo-EM structure of the yeast mitochondrial SAM-Tom40/Tom5/Tom6 complex at 3.0 angstrom
Summary for 7E4I
| Entry DOI | 10.2210/pdb7e4i/pdb |
| EMDB information | 30985 30986 |
| Descriptor | Sorting assembly machinery 50 kDa subunit, Sorting assembly machinery 35 kDa subunit, Sorting assembly machinery 37 kDa subunit, ... (6 entities in total) |
| Functional Keywords | translocase |
| Biological source | Saccharomyces cerevisiae S288c (Baker's yeast) More |
| Total number of polymer chains | 6 |
| Total formula weight | 189114.74 |
| Authors | Wang, Q.,Guan, Z.Y.,Qi, L.B.,Yan, C.Y.,Yin, P. (deposition date: 2021-02-13, release date: 2021-09-01, Last modification date: 2024-06-05) |
| Primary citation | 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, 373:1377-1381, 2021 Cited by 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 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. PubMed: 34446444DOI: 10.1126/science.abh0704 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.05 Å) |
Structure validation
Download full validation report
