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Open data
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Basic information
| Entry | Database: PDB / ID: 9jmk | |||||||||||||||||||||||||||||||||
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| Title | 50S Ribosomal Subunit precursor state III | |||||||||||||||||||||||||||||||||
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Keywords | RIBOSOME / 50S subunit / Precursor / Ribosome assembly intermediate | |||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationtranscriptional attenuation / endoribonuclease inhibitor activity / positive regulation of ribosome biogenesis / RNA-binding transcription regulator activity / negative regulation of cytoplasmic translation / DnaA-L2 complex / translation repressor activity / negative regulation of DNA-templated DNA replication initiation / mRNA regulatory element binding translation repressor activity / assembly of large subunit precursor of preribosome ...transcriptional attenuation / endoribonuclease inhibitor activity / positive regulation of ribosome biogenesis / RNA-binding transcription regulator activity / negative regulation of cytoplasmic translation / DnaA-L2 complex / translation repressor activity / negative regulation of DNA-templated DNA replication initiation / mRNA regulatory element binding translation repressor activity / assembly of large subunit precursor of preribosome / cytosolic ribosome assembly / response to reactive oxygen species / ribosome assembly / regulation of cell growth / DNA-templated transcription termination / response to radiation / mRNA 5'-UTR binding / large ribosomal subunit / transferase activity / ribosome binding / 5S rRNA binding / ribosomal large subunit assembly / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / response to antibiotic / negative regulation of DNA-templated transcription / mRNA binding / DNA binding / RNA binding / zinc ion binding / cytosol / cytoplasm Similarity search - Function | |||||||||||||||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4 Å | |||||||||||||||||||||||||||||||||
Authors | Sengupta, S. / Mukherjee, R. / Pilsl, M. / Bagale, S. / Adhikary, A.D. / Borkar, A. / Pradeepkumar, P.I. / Engel, C. / Chowdhury, A. / Kaushal, P.S. / Anand, R. | |||||||||||||||||||||||||||||||||
| Funding support | India, United Kingdom, 3items
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Citation | Journal: Sci Adv / Year: 2025Title: Mechanistic insights into 50 precursor recognition and targeting by erythromycin resistance methyltransferase. Authors: Sombuddha Sengupta / Rajat Mukherjee / Michael Pilsl / Siddharam Bagale / Arijit Das Adhikary / Aditi N Borkar / Pushpangadan Indira Pradeepkumar / Christoph Engel / Arindam Chowdhury / Prem ...Authors: Sombuddha Sengupta / Rajat Mukherjee / Michael Pilsl / Siddharam Bagale / Arijit Das Adhikary / Aditi N Borkar / Pushpangadan Indira Pradeepkumar / Christoph Engel / Arindam Chowdhury / Prem S Kaushal / Ruchi Anand / ![]() Abstract: Erythromycin resistance methyltransferases (Erms) confer resistance to macrolide, lincosamide, and streptogramin B antibiotics by methylating an internal base (A2058, numbering) in an elusive ...Erythromycin resistance methyltransferases (Erms) confer resistance to macrolide, lincosamide, and streptogramin B antibiotics by methylating an internal base (A2058, numbering) in an elusive precursor ribosomal state. Here, we capture the 50 ribosomal precursor-Erm complex by cryo-EM and show that a transient pocket formed in the early steps of ribosome biogenesis, situated 35 angstrom from the methylation site, serves as an anchor for the auxiliary C-terminal domain of Erm, thereby playing a crucial role in achieving specificity in this short-lived substrate with evolving structural features. Cryo-EM reveals that the catalytic Rossman fold of Erm undergoes a swaying motion to facilitate substrate scouting. Corroboratory smFRET studies show that for effective catalysis, Erm transitions between multiple conformations, an effective strategy adopted to orient the dynamic helix where methylation occurs. Unraveling this unique mechanism of targeting adopted by Erm paves the way for selective design of allosteric inhibitors directed toward reversing MLS resistance. | |||||||||||||||||||||||||||||||||
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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 | 9jmk.cif.gz | 1.7 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9jmk.ent.gz | 1.3 MB | Display | PDB format |
| PDBx/mmJSON format | 9jmk.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jm/9jmk ftp://data.pdbj.org/pub/pdb/validation_reports/jm/9jmk | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 61605MC ![]() 9jnsC ![]() 9jsrC 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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| 1 |
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Components
+50S ribosomal protein ... , 26 types, 26 molecules 0123CDEFGHJKLNOPQRSTUVWXYZ
-RNA chain , 2 types, 2 molecules AB
| #5: RNA chain | Mass: 941612.375 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #6: RNA chain | Mass: 38790.090 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-Details
| 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: 50S precursor state III / Type: RIBOSOME / Entity ID: all / Source: RECOMBINANT |
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| Source (natural) | Organism: ![]() |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K |
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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: 2500 nm / Nominal defocus min: 750 nm |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Electron dose: 41.25 e/Å2 / Film or detector model: GATAN K3 BIOCONTINUUM (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||
| Particle selection | Num. of particles selected: 205807 | ||||||||||||||||||||
| Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||
| 3D reconstruction | Resolution: 4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 6081 / Details: Final map deposited has been subjected LPF / Symmetry type: POINT | ||||||||||||||||||||
| Atomic model building | PDB-ID: 6GC8 Accession code: 6GC8 / Source name: PDB / Type: experimental model |
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About Yorodumi






India,
United Kingdom, 3items
Citation






PDBj































FIELD EMISSION GUN
