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Yorodumi- EMDB-71287: NAC H59-docked barrel: Ribosome nascent chain complex (Oxa1LdelMTS) -
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Open data
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Basic information
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| Title | NAC H59-docked barrel: Ribosome nascent chain complex (Oxa1LdelMTS) | |||||||||
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Keywords | NAC / mitochondrial sorting / Ribosome | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.08 Å | |||||||||
Authors | Maldosevic E / Jomaa A | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: Nat Commun / Year: 2026Title: A molecular switch in NAC prevents mitochondrial protein mistargeting by SRP. Authors: Emir Maldosevic / Radoslaw Jakub Gora / Liangguang Leo Lin / Linyao Elina Zhou / Zexin Jason Li / Yelena Peskova / Ling Qi / Shu-Ou Shan / Ahmad Jomaa / ![]() Abstract: The nascent polypeptide-associated complex (NAC) co-translationally screens all nascent proteins and regulates their access to signal recognition particle (SRP) to ensure the fidelity of protein ...The nascent polypeptide-associated complex (NAC) co-translationally screens all nascent proteins and regulates their access to signal recognition particle (SRP) to ensure the fidelity of protein targeting to the endoplasmic reticulum (ER). However, the mechanism by which NAC prevents the mistargeting of nascent mitochondrial proteins remains unclear. Here, we identify a molecular switch in NAC that allows its central barrel domain to adopt a stabilized conformation on ribosomes exposing a mitochondrial targeting sequence (MTS). Mutations of the MTS on the nascent chain or in the NAC switch region increase NAC barrel dynamics and reduce its binding to the ribosome. This impairs the ability of NAC to prevent mistargeting by SRP and causes ER stress in human cells. Our work reveals how NAC detects nascent mitochondrial proteins early in translation and prevents their promiscuous access to SRP, elucidating the structural basis that underlies this role and providing mechanistic insights into protein targeting fidelity with broader implications for cellular proteostasis. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_71287.map.gz | 483.7 MB | EMDB map data format | |
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| Header (meta data) | emd-71287-v30.xml emd-71287.xml | 14.1 KB 14.1 KB | Display Display | EMDB header |
| Images | emd_71287.png | 128.5 KB | ||
| Masks | emd_71287_msk_1.map | 512 MB | Mask map | |
| Filedesc metadata | emd-71287.cif.gz | 4.1 KB | ||
| Others | emd_71287_half_map_1.map.gz emd_71287_half_map_2.map.gz | 474.9 MB 475 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-71287 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-71287 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_71287.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.83 Å | ||||||||||||||||||||||||||||||||||||
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_71287_msk_1.map | ||||||||||||
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-Half map: #1
| File | emd_71287_half_map_1.map | ||||||||||||
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-Half map: #2
| File | emd_71287_half_map_2.map | ||||||||||||
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Sample components
-Entire : NAC (H59-docked barrel): Ribosome nascent chain complex (Oxa1LdelMTS)
| Entire | Name: NAC (H59-docked barrel): Ribosome nascent chain complex (Oxa1LdelMTS) |
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| Components |
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-Supramolecule #1: NAC (H59-docked barrel): Ribosome nascent chain complex (Oxa1LdelMTS)
| Supramolecule | Name: NAC (H59-docked barrel): Ribosome nascent chain complex (Oxa1LdelMTS) type: complex / ID: 1 / Parent: 0 |
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| Source (natural) | Organism: ![]() |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.5 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 40.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.4000000000000001 µm / Nominal defocus min: 0.8 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords
Authors
United States, 1 items
Citation


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Processing
FIELD EMISSION GUN
