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- PDB-9r91: Trimer TatBC complex with bound substrate SufI -

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Basic information

Entry
Database: PDB / ID: 9r91
TitleTrimer TatBC complex with bound substrate SufI
Components
  • Cell division protein FtsP
  • Sec-independent protein translocase protein TatB
  • Sec-independent protein translocase protein TatC
KeywordsTRANSLOCASE / membrane protein / twin-arginine 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 / FtsZ-dependent cytokinesis / cell division site / response to ionizing radiation / response to stress / transmembrane protein transporter activity / response to radiation ...proton motive force dependent protein transmembrane transporter activity / TAT protein transport complex / protein transport by the Tat complex / intracellular protein transmembrane transport / FtsZ-dependent cytokinesis / cell division site / response to ionizing radiation / response to stress / transmembrane protein transporter activity / response to radiation / outer membrane-bounded periplasmic space / response to oxidative stress / oxidoreductase activity / copper ion binding / cell division / protein homodimerization activity / membrane / identical protein binding / plasma membrane
Similarity search - Function
Cell division protein FtsP / Sec-independent protein translocase protein TatB / Sec-independent periplasmic protein translocase, conserved site / TatC family signature. / Sec-independent periplasmic protein translocase TatC / Sec-independent protein translocase protein (TatC) / Sec-independent protein translocase protein TatA/B/E / mttA/Hcf106 family / Twin-arginine translocation pathway, signal sequence, bacterial/archaeal / Multicopper oxidase, C-terminal ...Cell division protein FtsP / Sec-independent protein translocase protein TatB / Sec-independent periplasmic protein translocase, conserved site / TatC family signature. / Sec-independent periplasmic protein translocase TatC / Sec-independent protein translocase protein (TatC) / Sec-independent protein translocase protein TatA/B/E / mttA/Hcf106 family / Twin-arginine translocation pathway, signal sequence, bacterial/archaeal / Multicopper oxidase, C-terminal / Multicopper oxidase / Multicopper oxidase / Multicopper oxidase, N-terminal / Multicopper oxidase / Twin arginine translocation (Tat) signal profile. / Twin-arginine translocation pathway, signal sequence / Cupredoxin
Similarity search - Domain/homology
Cell division protein FtsP / Sec-independent protein translocase protein TatC / Sec-independent protein translocase protein TatB
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.7 Å
AuthorsZhao, Z. / Sazanov, L.
Funding support Austria, 1items
OrganizationGrant numberCountry
Other privatehttps://ist.ac.at/en/home Austria
CitationJournal: To Be Published
Title: Trimer TatBC complex with bound substrate SufI
Authors: Zhao, Z. / Sazanov, L.
History
DepositionMay 18, 2025Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 27, 2026Provider: repository / Type: Initial release
Revision 1.0May 27, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0May 27, 2026Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
Revision 1.0May 27, 2026Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0May 27, 2026Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0May 27, 2026Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0May 27, 2026Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Sec-independent protein translocase protein TatC
C: Sec-independent protein translocase protein TatC
B: Sec-independent protein translocase protein TatC
D: Sec-independent protein translocase protein TatB
E: Sec-independent protein translocase protein TatB
F: Sec-independent protein translocase protein TatB
G: Cell division protein FtsP


Theoretical massNumber of molelcules
Total (without water)203,6117
Polymers203,6117
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein Sec-independent protein translocase protein TatC / TatC-flag


Mass: 31758.975 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Details: flag tag / Source: (gene. exp.) Escherichia coli (E. coli) / Gene: tatC, mttB, yigU, yigV, b3839, JW3815 / Production host: Escherichia coli (E. coli) / References: UniProt: P69423
#2: Protein Sec-independent protein translocase protein TatB / TatB


Mass: 18441.818 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: tatB, mttA2, ysgB, b3838, JW5580 / Production host: Escherichia coli (E. coli) / References: UniProt: P69425
#3: Protein Cell division protein FtsP / Sufi-His8tag


Mass: 53009.020 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: His8tag / Source: (gene. exp.) Escherichia coli (E. coli) / Gene: ftsP, sufI, b3017, JW2985 / Production host: Escherichia coli (E. coli) / References: UniProt: P26648
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: twin-arginine translocase / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Molecular weightExperimental value: NO
Source (natural)Organism: Escherichia coli (E. coli)
Source (recombinant)Organism: Escherichia coli (E. coli)
Buffer solutionpH: 7.6
Details: 50 mM Tris-HCl pH7.6, 90 mM NaCl, 60 mM KCl, 0.2% Digitonin, 0.002% pmsf, protease inhibitor
Buffer component
IDConc.NameFormulaBuffer-ID
150 mMTrisTris1
290 mMsodium chlorideNaCl1
360 mMpotassium chlorideKCl1
SpecimenConc.: 0.25 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R0.6/1
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277.15 K

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 81000 X / Nominal defocus max: 2500 nm / Nominal defocus min: 1500 nm / Alignment procedure: COMA FREE
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingElectron dose: 80 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Num. of grids imaged: 1 / Num. of real images: 10177
EM imaging opticsEnergyfilter name: GIF Bioquantum / Energyfilter slit width: 20 eV

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Processing

EM software
IDNameVersionCategory
1RELION5particle selection
2EPUimage acquisition
4RELION5CTF correction
7Cootmodel fitting
9PHENIXdev_4933model refinement
10RELION5initial Euler assignment
11RELION5final Euler assignment
12RELION5classification
13Coot3D reconstruction
14PHENIXdev_4933+SVN3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 163739 / Algorithm: FOURIER SPACE / Num. of class averages: 1 / Symmetry type: POINT
RefinementHighest resolution: 3.7 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00410596
ELECTRON MICROSCOPYf_angle_d0.78614465
ELECTRON MICROSCOPYf_dihedral_angle_d13.8113798
ELECTRON MICROSCOPYf_chiral_restr0.0471708
ELECTRON MICROSCOPYf_plane_restr0.0071807

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