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Yorodumi- PDB-9gdp: Cryo-EM structure of Vibrio cholerae RNA polymerase holoenzyme bo... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9gdp | |||||||||||||||||||||||||||
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| Title | Cryo-EM structure of Vibrio cholerae RNA polymerase holoenzyme bound to an ompU promoter DNA fragment and 5-mer RNA | |||||||||||||||||||||||||||
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Keywords | TRANSCRIPTION / RNA polymerase / Open promoter complex / ompU / Vibrio cholerae | |||||||||||||||||||||||||||
| Function / homology | Function and homology informationsigma factor activity / DNA-directed RNA polymerase complex / DNA-templated transcription initiation / ribonucleoside binding / DNA-directed RNA polymerase / DNA-directed RNA polymerase activity / protein dimerization activity / DNA-templated transcription / magnesium ion binding / DNA binding ...sigma factor activity / DNA-directed RNA polymerase complex / DNA-templated transcription initiation / ribonucleoside binding / DNA-directed RNA polymerase / DNA-directed RNA polymerase activity / protein dimerization activity / DNA-templated transcription / magnesium ion binding / DNA binding / zinc ion binding / cytoplasm Similarity search - Function | |||||||||||||||||||||||||||
| Biological species | Vibrio cholerae O395 (bacteria) | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.6 Å | |||||||||||||||||||||||||||
Authors | Alcaide-Jimenez, A. / Baudin, F. / Canals, A. / Machon, C. / Murciano, B. / Fabrega-Ferrer, M. / Bantysh, O. / Perez-Luque, R. / Krukonis, E.S. / Muller, C.W. / Coll, M. | |||||||||||||||||||||||||||
| Funding support | Spain, 2items
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Citation | Journal: Sci Adv / Year: 2026Title: Structures of transcription complexes reveal how ToxR and TcpP recruit the RNA polymerase and activate virulence genes. Authors: Adrià Alcaide-Jiménez / Albert Canals / Florence Baudin / Cristina Machón / Montserrat Fàbrega-Ferrer / Olga Bantysh / Rosa Pérez-Luque / Brice Murciano / Ali A Mohammad / Michael J ...Authors: Adrià Alcaide-Jiménez / Albert Canals / Florence Baudin / Cristina Machón / Montserrat Fàbrega-Ferrer / Olga Bantysh / Rosa Pérez-Luque / Brice Murciano / Ali A Mohammad / Michael J Rowse / Joseph M Ferracciolo / Eric S Krukonis / Christoph W Müller / Miquel Coll / ![]() Abstract: Activation of virulence in , the etiological agent of cholera disease, is mediated by two transmembrane one-component signal-transduction proteins, ToxR and TcpP, which are also transcription factors. ...Activation of virulence in , the etiological agent of cholera disease, is mediated by two transmembrane one-component signal-transduction proteins, ToxR and TcpP, which are also transcription factors. Using cryo-electron microscopy, we have solved five structures of the and transcription activation complexes, including the RNA polymerase (RNAP) holoenzyme, promoter DNAs, transcribed RNA, and their corresponding transcription factors, ToxR or TcpP and ToxR-TcpP, respectively. Activation is achieved through the interaction of ToxR or TcpP with the α-C-terminal repeat domain of RNAP where a single residue of the activator, a phenylalanine, appears to be the most critical contact, as confirmed by mutagenesis. No interactions of the transcription factors were observed with other subunits of the RNAP, i.e., the σ subunit as it occurs in the structurally related PhoB family of two-component transcription factors. The structures, and their comparison with our previously solved DNA promoter-ToxR x-ray structures, unveil the molecular mechanism of cholera virulence gene activation. | |||||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9gdp.cif.gz | 775.1 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9gdp.ent.gz | 607 KB | Display | PDB format |
| PDBx/mmJSON format | 9gdp.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gd/9gdp ftp://data.pdbj.org/pub/pdb/validation_reports/gd/9gdp | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 51274MC ![]() 9gdoC ![]() 9gdqC ![]() 9gdrC ![]() 9gdsC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-DNA-directed RNA polymerase subunit ... , 4 types, 6 molecules CDEABG
| #1: Protein | Mass: 149696.531 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Vibrio cholerae O395 (bacteria) / Gene: rpoB, VC0395_A2730, VC395_0371 / Production host: ![]() |
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| #2: Protein | Mass: 155234.281 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Vibrio cholerae O395 (bacteria) / Gene: rpoC, VC0395_A2731, VC395_0372 / Production host: ![]() |
| #3: Protein | Mass: 10068.355 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Vibrio cholerae O395 (bacteria) / Gene: rpoZ, VC0395_A2281, VC395_2821 / Production host: ![]() |
| #4: Protein | Mass: 36461.473 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Vibrio cholerae O395 (bacteria) / Gene: rpoA, VC0395_A2149, VC395_2684 / Production host: ![]() |
-OmpU promoter ... , 2 types, 2 molecules TL
| #7: DNA chain | Mass: 21329.688 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Vibrio cholerae O395 (bacteria) |
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| #8: DNA chain | Mass: 21109.568 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Vibrio cholerae O395 (bacteria) / References: GenBank: 657184927 |
-Protein / RNA chain , 2 types, 2 molecules FH
| #5: Protein | Mass: 70749.648 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Vibrio cholerae O395 (bacteria) / Gene: rpoD, VC0395_A0044 / Production host: ![]() |
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| #6: RNA chain | Mass: 1594.032 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Vibrio cholerae O395 (bacteria) |
-Non-polymers , 2 types, 3 molecules 


| #9: Chemical | | #10: Chemical | ChemComp-MG / | |
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-Details
| Has ligand of interest | N |
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| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
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| Molecular weight | Experimental value: NO | ||||||||||||||||||||||||||||||
| Source (natural) |
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| Source (recombinant) |
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| Buffer solution | pH: 8 Details: 10 mM HEPES pH 8.0, 500 mM NaCl, 1 mM DTT and 0.1 mM EDTA, CHAPSO 4mM | ||||||||||||||||||||||||||||||
| Specimen | Conc.: 3 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1800 nm / Nominal defocus min: 700 nm |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
| EM software | Name: PHENIX / Version: 1.21_5207 / Category: model refinement |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
| 3D reconstruction | Resolution: 2.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 123792 / Symmetry type: POINT |
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Vibrio cholerae O395 (bacteria)
Spain, 2items
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FIELD EMISSION GUN