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Open data
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Basic information
| Entry | Database: PDB / ID: 9kq0 | |||||||||||||||||||||||||||
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| Title | Structure of TolQRA complex at pH 8.0 from E.coli | |||||||||||||||||||||||||||
Components |
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Keywords | MEMBRANE PROTEIN / TolQRA / TolQ / TolR / TolA / Tol-Pal complex / Proton motive force / proton transporter | |||||||||||||||||||||||||||
| Function / homology | Function and homology informationcellular response to bacteriocin / regulation of membrane invagination / cell septum assembly / bacteriocin transport / SUMO is conjugated to E1 (UBA2:SAE1) / SUMOylation of nuclear envelope proteins / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / SUMO is proteolytically processed / toxin transmembrane transporter activity / SUMOylation of transcription factors ...cellular response to bacteriocin / regulation of membrane invagination / cell septum assembly / bacteriocin transport / SUMO is conjugated to E1 (UBA2:SAE1) / SUMOylation of nuclear envelope proteins / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / SUMO is proteolytically processed / toxin transmembrane transporter activity / SUMOylation of transcription factors / Postmitotic nuclear pore complex (NPC) reformation / SUMOylation of transcription cofactors / septin ring / SUMOylation of DNA damage response and repair proteins / Transcriptional and post-translational regulation of MITF-M expression and activity / SUMOylation of DNA replication proteins / SUMOylation of SUMOylation proteins / protein import / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / virion binding / SUMOylation of RNA binding proteins / cell envelope / SUMOylation of chromatin organization proteins / cell division site / ubiquitin-like protein ligase binding / protein sumoylation / transmembrane transporter activity / condensed nuclear chromosome / protein tag activity / disordered domain specific binding / protein transport / protein domain specific binding / cell division / symbiont entry into host cell / identical protein binding / membrane / nucleus / plasma membrane Similarity search - Function | |||||||||||||||||||||||||||
| Biological species | ![]() ![]() | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.6 Å | |||||||||||||||||||||||||||
Authors | Dong, C. / Zhang, Z. | |||||||||||||||||||||||||||
| Funding support | China, 1items
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Citation | Journal: To Be PublishedTitle: Structure of TolQRA complex at pH 8.0 from E.coli Authors: Dong, C. / Zhang, Z. | |||||||||||||||||||||||||||
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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 | 9kq0.cif.gz | 266.9 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9kq0.ent.gz | 194.6 KB | Display | PDB format |
| PDBx/mmJSON format | 9kq0.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kq/9kq0 ftp://data.pdbj.org/pub/pdb/validation_reports/kq/9kq0 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 62493MC 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
| #1: Protein | Mass: 25779.844 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Protein | Mass: 15398.884 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #3: Protein | Mass: 58492.613 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: SMT3, YDR510W, D9719.15, tolA, cim, excC, lky, b0739, JW0729 Strain: MG1655 / Production host: ![]() Has protein modification | N | |
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-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
| Component | Name: Tol-Pal system complex TolQRA / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT | |||||||||||||||
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| Source (natural) |
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| Source (recombinant) | Organism: ![]() | |||||||||||||||
| Buffer solution | pH: 8 | |||||||||||||||
| Specimen | 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: OTHER |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 1200 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 160613 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 3.6 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi







China, 1items
Citation

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FIELD EMISSION GUN