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- EMDB-71310: NAC: ribosome nascent chain complex (Hsp60) -

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Basic information

Entry
Database: EMDB / ID: EMD-71310
TitleNAC: ribosome nascent chain complex (Hsp60)
Map data
Sample
  • Complex: NAC: Ribosome nascent chain complex(Hsp60)
KeywordsNAC / mitochondrial sorting / RIBOSOME
Biological speciesOryctolagus cuniculus (rabbit)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.04 Å
AuthorsMaldosevic E / Jomaa A
Funding support United States, 2 items
OrganizationGrant numberCountry
American Cancer Society United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) United States
CitationJournal: bioRxiv / Year: 2025
Title: A molecular switch in NAC prevents mitochondrial protein mistargeting by SRP.
Authors: Emir Maldosevic / Radoslaw 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 the 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 the 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 identified 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 increases NAC barrel dynamics and reduces its binding to the ribosome. This leads to an impaired 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 novel insights into protein targeting fidelity with broader implications for cellular proteostasis.
History
DepositionJun 19, 2025-
Header (metadata) releaseAug 20, 2025-
Map releaseAug 20, 2025-
UpdateAug 20, 2025-
Current statusAug 20, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_71310.png

Downloads & links

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Map

FileDownload / File: emd_71310.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.17 Å/pix.
x 512 pix.
= 599.04 Å		1.17 Å/pix.
x 512 pix.
= 599.04 Å		1.17 Å/pix.
x 512 pix.
= 599.04 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.17 Å
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Histogram

Histogram (log scale)
Contour LevelBy EMDB: 0.12
Minimum - Maximum-0.28846484 - 0.59594023
Average (Standard dev.)-0.00032047264 (±0.021788418)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions512512512
Spacing512512512
CellA=B=C: 599.04 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_71310_msk_1.map
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Half map: #1

Fileemd_71310_half_map_1.map
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Half map: #2

Fileemd_71310_half_map_2.map
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Sample components

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Entire : NAC: Ribosome nascent chain complex(Hsp60)

EntireName: NAC: Ribosome nascent chain complex(Hsp60)
Components
  • Complex: NAC: Ribosome nascent chain complex(Hsp60)

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Supramolecule #1: NAC: Ribosome nascent chain complex(Hsp60)

SupramoleculeName: NAC: Ribosome nascent chain complex(Hsp60) / type: complex / ID: 1 / Parent: 0
Source (natural)Organism: Oryctolagus cuniculus (rabbit)

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS GLACIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.2 µm / Nominal defocus min: 1.2 µm

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Image processing

CTF correctionType: NONE
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.04 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 36986
Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: PROJECTION MATCHING

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