[English] 日本語
Yorodumi- PDB-10fz: 30S ribosomal subunit from E. coli missing the gene encoding for ... -
+
Open data
-
Basic information
| Entry | Database: PDB / ID: 10fz | |||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Title | 30S ribosomal subunit from E. coli missing the gene encoding for the 16S rRNA 2'-O-methyltransferase RsmI | |||||||||||||||||||||||||||
Components |
| |||||||||||||||||||||||||||
Keywords | RIBOSOME / methylation / 30S subunit / helix 44 / RsmI | |||||||||||||||||||||||||||
| Function / homology | Function and homology informationtranscription antitermination factor activity, RNA binding / ornithine decarboxylase inhibitor activity / misfolded RNA binding / Group I intron splicing / RNA folding / four-way junction DNA binding / regulation of mRNA stability / negative regulation of translational initiation / mRNA regulatory element binding translation repressor activity / regulation of DNA-templated transcription elongation ...transcription antitermination factor activity, RNA binding / ornithine decarboxylase inhibitor activity / misfolded RNA binding / Group I intron splicing / RNA folding / four-way junction DNA binding / regulation of mRNA stability / negative regulation of translational initiation / mRNA regulatory element binding translation repressor activity / regulation of DNA-templated transcription elongation / positive regulation of RNA splicing / transcription elongation factor complex / transcription antitermination / DNA endonuclease activity / DNA-templated transcription termination / maintenance of translational fidelity / mRNA 5'-UTR binding / regulation of translation / ribosome biogenesis / ribosomal small subunit assembly / ribosomal small subunit biogenesis / small ribosomal subunit / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / response to antibiotic / hydrolase activity / mRNA binding / RNA binding / zinc ion binding / membrane / cytoplasm / cytosol Similarity search - Function | |||||||||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.91 Å | |||||||||||||||||||||||||||
Authors | Barmada, M.I. / Nandi, S. / Conn, G.L. | |||||||||||||||||||||||||||
| Funding support | United States, 3items
| |||||||||||||||||||||||||||
Citation | Journal: To Be PublishedTitle: Mechanism of 30S subunit recognition and modification by the conserved bacterial ribosomal RNA methyltransferase RsmI Authors: Barmada, M.I. / McGinity, E.N. / Nandi, S. / Dey, D. / Zelinskaya, N. / Harris, G.M. / Comstock, L.R. / Dunham, C.M. / Conn, G.L. | |||||||||||||||||||||||||||
| History |
|
-
Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
|---|
-
Downloads & links
-
Download
| PDBx/mmCIF format | 10fz.cif.gz | 1.4 MB | Display | PDBx/mmCIF format |
|---|---|---|---|---|
| PDB format | pdb10fz.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 10fz.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/0f/10fz ftp://data.pdbj.org/pub/pdb/validation_reports/0f/10fz | HTTPS FTP |
|---|
-Related structure data
| Related structure data | ![]() 75144MC M: map data used to model this data C: citing same article ( |
|---|---|
| Similar structure data | Similarity search - Function & homology F&H Search |
-
Links
-
Assembly
| Deposited unit | ![]()
|
|---|---|
| 1 |
|
-
Components
-RNA chain , 1 types, 1 molecules A
| #1: RNA chain | Mass: 499690.031 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
|---|
-Small ribosomal subunit protein ... , 20 types, 20 molecules DEFHKLOPQRTBUCGIJMNS
| #2: Protein | Mass: 23383.002 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
|---|---|
| #3: Protein | Mass: 17498.203 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #4: Protein | Mass: 15727.512 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #5: Protein | Mass: 14015.361 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #6: Protein | Mass: 13739.778 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #7: Protein | Mass: 13636.961 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #8: Protein | Mass: 10319.882 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #9: Protein | Mass: 9207.572 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #10: Protein | Mass: 9593.296 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #11: Protein | Mass: 8874.276 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #12: Protein | Mass: 9577.268 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #13: Protein | Mass: 26650.475 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #14: Protein | Mass: 8524.039 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #15: Protein | Mass: 25900.117 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #16: Protein | Mass: 19923.959 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #17: Protein | Mass: 14755.074 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #18: Protein | Mass: 11755.597 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #19: Protein | Mass: 12997.271 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #20: Protein | Mass: 11475.364 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #21: Protein | Mass: 10324.160 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Non-polymers , 2 types, 109 molecules 


| #22: Chemical | ChemComp-MG / #23: Water | ChemComp-HOH / | |
|---|
-Details
| Has ligand of interest | N |
|---|---|
| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
|---|---|
| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-
Sample preparation
| Component | Name: small ribosomal subunit from a delta rsmI E. coli strain Type: RIBOSOME Details: E. coli 30S subunit lacking Cm1402 modification. This map was generated as part of an EM sample containing the complex of the 16S 2'-O-methyltransferase RsmI and the delta rsmI 30S (PDB ...Details: E. coli 30S subunit lacking Cm1402 modification. This map was generated as part of an EM sample containing the complex of the 16S 2'-O-methyltransferase RsmI and the delta rsmI 30S (PDB 9PZG/EMDB 72071). Particles with no enzyme occupancy were isolated to generate the map of the unbound delta rsmI 30S subunit. Entity ID: #1-#21 / Source: NATURAL |
|---|---|
| Molecular weight | Value: 0.85 MDa / Experimental value: NO |
| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.6 Details: 10 mM HEPES, 10 mM MgCl2, 100 mM NH4Cl, 6 mM Beta-mercaptoethanol |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES Details: Recombinant RsmI (1.2 uM), delta-rsmI 30S (0.4 uM), and the SAM analog NM6 (24 uM) were incubated for 30 minutes at 37C to prepare the complex. |
| Specimen support | Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: C-flat-1.2/1.3 |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277.15 K |
-
Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
|---|---|
| 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 magnification: 105000 X / Nominal defocus max: 2900 nm / Nominal defocus min: 400 nm / Cs: 2.7 mm |
| Specimen holder | Cryogen: NITROGEN |
| Image recording | Average exposure time: 1.8 sec. / Electron dose: 49.27 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Num. of grids imaged: 1 / Num. of real images: 8164 |
-
Processing
| EM software |
| ||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||
| Particle selection | Num. of particles selected: 3781314 | ||||||||||||||||||||
| 3D reconstruction | Resolution: 2.91 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 58273 / Symmetry type: POINT | ||||||||||||||||||||
| Atomic model building | Protocol: FLEXIBLE FIT / Space: REAL | ||||||||||||||||||||
| Atomic model building | PDB-ID: 7oe1 Accession code: 7oe1 / Source name: PDB / Type: experimental model | ||||||||||||||||||||
| Refinement | Cross valid method: NONE |
Movie
Controller
About Yorodumi





United States, 3items
Citation

PDBj































FIELD EMISSION GUN
