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- EMDB-39090: Structure of the SecA-SecY complex with the substrate FtsQ-LacY(+... -

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Basic information

Entry
Database: EMDB / ID: EMD-39090
TitleStructure of the SecA-SecY complex with the substrate FtsQ-LacY(+7C) treated with DTT
Map data
Sample
  • Complex: SecA-SecY complex with the substrate FtsQ-LacY(+7C) treated with DTT
    • Protein or peptide: Protein translocase subunit SecY
    • Protein or peptide: Protein translocase subunit SecE
    • Protein or peptide: Cell division protein FtsQ,Lactose permease
KeywordsProtein translocation / Membrane protein insertion / Protein chaperone / PROTEIN TRANSPORT
Function / homology
Function and homology information


lactose:proton symporter activity / lactose transport / FtsQBL complex / carbohydrate:proton symporter activity / divisome complex / lactose binding / intracellular protein transmembrane transport / protein transport by the Sec complex / division septum assembly / FtsZ-dependent cytokinesis ...lactose:proton symporter activity / lactose transport / FtsQBL complex / carbohydrate:proton symporter activity / divisome complex / lactose binding / intracellular protein transmembrane transport / protein transport by the Sec complex / division septum assembly / FtsZ-dependent cytokinesis / cell division site / carbohydrate transport / protein secretion / protein transmembrane transporter activity / protein targeting / cell division / identical protein binding / membrane / plasma membrane
Similarity search - Function
LacY/RafB permease family / LacY/RafB permease family, conserved site / LacY proton/sugar symporter / LacY family proton/sugar symporters signature 1. / LacY family proton/sugar symporters signature 2. / Cell division protein FtsQ / Cell division protein FtsQ, C-terminal / Cell division protein FtsQ/DivIB, C-terminal / POTRA domain, FtsQ-type / Cell division protein FtsQ/DivIB, C-terminal ...LacY/RafB permease family / LacY/RafB permease family, conserved site / LacY proton/sugar symporter / LacY family proton/sugar symporters signature 1. / LacY family proton/sugar symporters signature 2. / Cell division protein FtsQ / Cell division protein FtsQ, C-terminal / Cell division protein FtsQ/DivIB, C-terminal / POTRA domain, FtsQ-type / Cell division protein FtsQ/DivIB, C-terminal / POTRA domain, FtsQ-type / SecE subunit of protein translocation complex, bacterial-like / SecE superfamily / Protein translocase subunit SecY / Protein secE/sec61-gamma signature. / Protein secY signature 1. / Protein secY signature 2. / SecE/Sec61-gamma subunits of protein translocation complex / Protein translocase complex, SecE/Sec61-gamma subunit / SecY/SEC61-alpha family / SecY domain superfamily / SecY conserved site / SecY / POTRA domain / POTRA domain profile. / Major facilitator superfamily domain / Major facilitator superfamily (MFS) profile. / MFS transporter superfamily
Similarity search - Domain/homology
Protein translocase subunit SecE / Protein translocase subunit SecY / Lactose permease / Cell division protein FtsQ
Similarity search - Component
Biological speciesGeobacillus thermodenitrificans NG80-2 (bacteria) / Escherichia coli K-12 (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.27 Å
AuthorsOu X / Ma C / Sun D / Xu J / Wu X / Gao N / Li L
Funding support China, 3 items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China)2019YFA0508900,2016YFA0500401 China
National Natural Science Foundation of China (NSFC)31725007,31630087,31800625,21873006,31870835 China
Other government2018M631249,2019M650327
CitationJournal: Cell / Year: 2025
Title: SecY translocon chaperones protein folding during membrane protein insertion.
Authors: Xiaomin Ou / Chengying Ma / Dongjie Sun / Jinkun Xu / Yang Wang / Xiaofei Wu / Dali Wang / Song Yang / Ning Gao / Chen Song / Long Li /
Abstract: The Sec translocon is vital for guiding membrane protein insertion into lipid bilayers. The insertion and folding processes of membrane proteins are poorly understood. Here, we report cryo-electron ...The Sec translocon is vital for guiding membrane protein insertion into lipid bilayers. The insertion and folding processes of membrane proteins are poorly understood. Here, we report cryo-electron microscopy structures of multi-spanning membrane proteins inserting through the SecY channel, the Sec translocon in prokaryotes. The high-resolution structures illustrate how bulky amino acids pass the narrow channel restriction. Comparison of different translocation states reveals that the cytoplasmic and extracellular cavities of the channel create distinct environments for promoting the unfolding and folding of transmembrane segments (TMs), respectively. Released substrate TMs are either flexible or stabilized by an unexpected hydrophilic groove between TM3 and TM4 of SecY. Disruption of the groove causes global defects in the folding of the membrane proteome. These findings demonstrate that beyond its role as a passive protein-conducting channel, the SecY translocon actively serves as a chaperone, employing multiple mechanisms to promote membrane protein insertion and folding.
History
DepositionFeb 7, 2024-
Header (metadata) releaseFeb 26, 2025-
Map releaseFeb 26, 2025-
UpdateApr 16, 2025-
Current statusApr 16, 2025Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_39090.png

Downloads & links

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Map

FileDownload / File: emd_39090.map.gz / Format: CCP4 / Size: 52.7 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.)
1.05 Å/pix.
x 240 pix.
= 252.48 Å		1.05 Å/pix.
x 240 pix.
= 252.48 Å		1.05 Å/pix.
x 240 pix.
= 252.48 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.052 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.02
Minimum - Maximum-0.03354773 - 0.09375
Average (Standard dev.)0.00018772032 (±0.001965182)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions240240240
Spacing240240240
CellA=B=C: 252.48001 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_39090_msk_1.map
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Half map: #2

Fileemd_39090_half_map_1.map
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Half map: #1

Fileemd_39090_half_map_2.map
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Sample components

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Entire : SecA-SecY complex with the substrate FtsQ-LacY(+7C) treated with DTT

EntireName: SecA-SecY complex with the substrate FtsQ-LacY(+7C) treated with DTT
Components
  • Complex: SecA-SecY complex with the substrate FtsQ-LacY(+7C) treated with DTT
    • Protein or peptide: Protein translocase subunit SecY
    • Protein or peptide: Protein translocase subunit SecE
    • Protein or peptide: Cell division protein FtsQ,Lactose permease

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Supramolecule #1: SecA-SecY complex with the substrate FtsQ-LacY(+7C) treated with DTT

SupramoleculeName: SecA-SecY complex with the substrate FtsQ-LacY(+7C) treated with DTT
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Geobacillus thermodenitrificans NG80-2 (bacteria)

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Macromolecule #1: Protein translocase subunit SecY

MacromoleculeName: Protein translocase subunit SecY / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Geobacillus thermodenitrificans NG80-2 (bacteria)
Molecular weightTheoretical: 47.512051 KDa
Recombinant expressionOrganism: Escherichia coli K-12 (bacteria)
SequenceString: MFRTISNFMR VSDIRNKIIF TLLMLIVFRI GTFIPVPSVN TDVLKLQDQL NAFGVLNIFC GGALQNFSIF AMGVMPYITA SIIVQLLQM DVVPKFAEWS KQGEMGRRKL AQFTRYFTIV LGFIQALGMS YGFNNLAGGM LIQNPGIGTY LLIAVVLTAG T AFLMWLGE ...String:
MFRTISNFMR VSDIRNKIIF TLLMLIVFRI GTFIPVPSVN TDVLKLQDQL NAFGVLNIFC GGALQNFSIF AMGVMPYITA SIIVQLLQM DVVPKFAEWS KQGEMGRRKL AQFTRYFTIV LGFIQALGMS YGFNNLAGGM LIQNPGIGTY LLIAVVLTAG T AFLMWLGE QITAKGVGNG ISIIIFAGIV SGIPTILNQI YAQTFENVGE DLTLNIVRLL LVALAVVAVI VGVIYIQQAF RK IPIQYAK RLEGRNPVGG HSTHLPLKVN PAGVIPVIFA VSFLIAPPTI ASFFGTNDVT LWIRRTFDYT HPVGMTIYVV LII AFTYFY AFVQVNPEQM ADNLKKQGGY IPGIRPGKNT QEYVTRILYR LTLVGSLFLA FIAVLPVFFV NFANLPPSAQ IGGT SLLIV VGVALETMKQ LESQLVKRHY RGFIK

UniProtKB: Protein translocase subunit SecY

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Macromolecule #2: Protein translocase subunit SecE

MacromoleculeName: Protein translocase subunit SecE / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Geobacillus thermodenitrificans NG80-2 (bacteria)
Molecular weightTheoretical: 8.2496 KDa
Recombinant expressionOrganism: Escherichia coli K-12 (bacteria)
SequenceString:
MQRVTNFFKE VVRELKKVSW PNRKELVNYT AVVLATVAFF TVFFAVIDLG ISQLIRLVFE GGHHHHHHHH

UniProtKB: Protein translocase subunit SecE

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Macromolecule #3: Cell division protein FtsQ,Lactose permease

MacromoleculeName: Cell division protein FtsQ,Lactose permease / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli K-12 (bacteria)
Molecular weightTheoretical: 8.272546 KDa
Recombinant expressionOrganism: Escherichia coli K-12 (bacteria)
SequenceString:
MAKKTILFLL TVLTTVLVSG WVVLGAQYED GCSGVVILKT LHMFEVPFLL VGAFSISGDG DSPHSYHSGD GDKLPEGV

UniProtKB: Cell division protein FtsQ, Lactose permease

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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
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 64.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: EMDB MAP
EMDB ID:

9731

Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.27 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 123581
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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