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- EMDB-47351: Cryo-EM structure of a TatAC complex from Nitratifractor salsuginis -

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Basic information

Entry
Database: EMDB / ID: EMD-47351
TitleCryo-EM structure of a TatAC complex from Nitratifractor salsuginis
Map datadeepEMhanced map used for model refinement
Sample
  • Complex: TatAC complex
    • Protein or peptide: Sec-independent protein translocase protein TatA
    • Protein or peptide: Sec-independent protein translocase protein TatC
KeywordsMembrane Protein / TatC / TatA / twin-arginine translocation / TRANSLOCASE
Function / homology
Function and homology information


proton motive force dependent protein transmembrane transporter activity / TAT protein transport complex / protein transport by the Tat complex / intracellular protein transmembrane transport / protein transmembrane transporter activity
Similarity search - Function
Sec-independent protein translocase protein TatA/E / Sec-independent periplasmic protein translocase, conserved site / TatC family signature. / Sec-independent protein translocase protein TatA/B/E / mttA/Hcf106 family / Sec-independent periplasmic protein translocase TatC / Sec-independent protein translocase protein (TatC)
Similarity search - Domain/homology
Sec-independent protein translocase protein TatA / Sec-independent protein translocase protein TatC
Similarity search - Component
Biological speciesNitratifractor salsuginis (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsDeme JC / Bryant OJ / Berks BC / Lea SM
Funding support United Kingdom, United States, 3 items
OrganizationGrant numberCountry
Medical Research Council (MRC, United Kingdom)MR/L000776/1 United Kingdom
Wellcome Trust107929/Z/15/Z United Kingdom
National Institutes of Health/National Cancer Institute (NIH/NCI)Intramural Research Program United States
CitationJournal: To Be Published
Title: Structure of the twin-arginine protein translocation pathway core complex and the molecular basis for substrate recognition
Authors: Deme JC / Bryant OJ / Berks BC / Lea SM
History
DepositionOct 17, 2024-
Header (metadata) releaseAug 27, 2025-
Map releaseAug 27, 2025-
UpdateAug 27, 2025-
Current statusAug 27, 2025Processing site: RCSB / Status: Released

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Structure visualization

Downloads & links

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Map

FileDownload / File: emd_47351.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationdeepEMhanced map used for model refinement
Voxel sizeX=Y=Z: 0.832 Å
Density
Contour LevelBy AUTHOR: 0.1
Minimum - Maximum-0.06365054 - 1.712166
Average (Standard dev.)0.0008531371 (±0.019865766)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions320320320
Spacing320320320
CellA=B=C: 266.24 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : TatAC complex

EntireName: TatAC complex
Components
  • Complex: TatAC complex
    • Protein or peptide: Sec-independent protein translocase protein TatA
    • Protein or peptide: Sec-independent protein translocase protein TatC

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Supramolecule #1: TatAC complex

SupramoleculeName: TatAC complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Nitratifractor salsuginis (bacteria)

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Macromolecule #1: Sec-independent protein translocase protein TatA

MacromoleculeName: Sec-independent protein translocase protein TatA / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Nitratifractor salsuginis (bacteria)
Molecular weightTheoretical: 9.367679 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MGMPSGWELL LVVGVIVLLF GGKKIPELAK GLGKGIKDFK QAVKEDEEAS APAKEIENKE ASASGTQSEA SEVKESQKAW SHPQFEK

UniProtKB: Sec-independent protein translocase protein TatA

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Macromolecule #2: Sec-independent protein translocase protein TatC

MacromoleculeName: Sec-independent protein translocase protein TatC / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Nitratifractor salsuginis (bacteria)
Molecular weightTheoretical: 42.954797 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MFESMKPHLA ELRQRLAISV LAVFVGFIIA FTFHNAILGW ITKPLNNALI QVGKIVEKRE MGTWKISGNE HNATLAPSKS PALLSDHAQ SAEKLHRTLA EASQATQNPK LQKLLSQAAS AAEELARNSR ILRKALVKEE NLTRQAVNQN LREKSFNGMI T THQVGGAF ...String:
MFESMKPHLA ELRQRLAISV LAVFVGFIIA FTFHNAILGW ITKPLNNALI QVGKIVEKRE MGTWKISGNE HNATLAPSKS PALLSDHAQ SAEKLHRTLA EASQATQNPK LQKLLSQAAS AAEELARNSR ILRKALVKEE NLTRQAVNQN LREKSFNGMI T THQVGGAF FVALKVSFFA GILMAMPVIL WQLWLFIAPG LYDNEKKMVL PFVVGGSVMF LIGVLFAYYV VTPFGFQFLI TF GSFLYTP LINIEDYVGF FTKILIGFGI AFELPVVAYF LALLGLITDK TLKDYFKYAI VIIFLLAAFL TPPDVLTQLL MAA PLILLY GLSILIVHYV NPYKPEEKED DEEEEEDEFE KAEREFEALE KGSESHESGS ENLYFQ

UniProtKB: Sec-independent protein translocase protein TatC

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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: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 51.1 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: 0.8 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 75284
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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