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| 001 | 641981 | ||
| 005 | 20260202210336.0 | ||
| 024 | 7 | _ | |a 10.1038/s41467-025-66417-0 |2 doi |
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| 100 | 1 | _ | |a Diederichs, Kathryn A. |0 0000-0001-9444-9797 |b 0 |
| 245 | _ | _ | |a The dynamic lateral gate of the mitochondrial β-barrel biogenesis machinery is blocked by darobactin A |
| 260 | _ | _ | |a [London] |c 2025 |b Springer Nature |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 520 | _ | _ | |a The folding and insertion of β-barrel proteins into the mitochondrial outer membrane is facilitated by the sorting and assembly machinery (SAM) complex. Here we report two 2.8 Å cryo-EM structures of the Thermothelomyces thermophilus SAM complex in the absence of substrate in which the Sam50 lateral gate adopts two different conformations: the first is a closed lateral gate as observed in previously published structures, while the second contains a Sam50 with the first four β-strands rotated outwards by approximately 45°, resulting in an open lateral gate. The observed monomeric open conformation contrasts our previous work where the open conformation was adopted by non-physiological up-down dimers. To understand how these lateral gate dynamics are influenced by substrate, we studied the interaction of the SAM complex with a β-signal peptide mimic, darobactin A. Darobactin A binds to the SAM complex with nanomolar affinity and inhibits the import and assembly of mitochondrial β-barrel proteins in vitro. Lastly, we solved a 3.0 Å cryo-EM structure of the Thermothelomyces thermophilus SAM complex bound to darobactin A, which reveals that darobactin A stabilizes the Sam50 lateral gate similar to the open conformation by binding to strand β1, therefore blocking β-barrel biogenesis. |
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| 700 | 1 | _ | |a Botos, Istvan |0 0000-0002-7702-6749 |b 1 |
| 700 | 1 | _ | |a Hayashi, Scout |0 0000-0002-6376-3860 |b 2 |
| 700 | 1 | _ | |a Gutishvili, Gvantsa |0 0000-0001-5681-8539 |b 3 |
| 700 | 1 | _ | |a Kotov, Vadim |0 P:(DE-H253)PIP1082976 |b 4 |
| 700 | 1 | _ | |a Kuo, Katie |0 0009-0001-5682-6173 |b 5 |
| 700 | 1 | _ | |a Iinishi, Akira |b 6 |
| 700 | 1 | _ | |a Cooper, Gwendolyn |0 0000-0003-3548-3551 |b 7 |
| 700 | 1 | _ | |a Schwarz, Benjamin |0 0000-0002-5894-953X |b 8 |
| 700 | 1 | _ | |a Celia, Herve |0 0000-0003-1203-8586 |b 9 |
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| 700 | 1 | _ | |a Lewis, Kim |0 0000-0002-1335-9982 |b 11 |
| 700 | 1 | _ | |a Gumbart, James C. |0 0000-0002-1510-7842 |b 12 |
| 700 | 1 | _ | |a Mindell, Joseph A. |0 P:(DE-HGF)0 |b 13 |e Corresponding author |
| 700 | 1 | _ | |a Buchanan, Susan K. |0 P:(DE-HGF)0 |b 14 |e Corresponding author |
| 773 | _ | _ | |a 10.1038/s41467-025-66417-0 |g Vol. 16, no. 1, p. 11349 |0 PERI:(DE-600)2553671-0 |n 1 |p 11349 |t Nature Communications |v 16 |y 2025 |x 2041-1723 |
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