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- PDB-9d89: E. coli 50S ribosomal subunit in complex with PrAMP rumicidin-2 (... -
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Open data
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Basic information
Entry | Database: PDB / ID: 9d89 | |||||||||||||||||||||||||||
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Title | E. coli 50S ribosomal subunit in complex with PrAMP rumicidin-2 (focused refinement) | |||||||||||||||||||||||||||
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![]() | RIBOSOME / Proline-rich antimicrobial peptides / PrAMP / Cryo-EM | |||||||||||||||||||||||||||
Function / homology | ![]() DnaA-L2 complex / negative regulation of DNA-templated DNA replication initiation / assembly of large subunit precursor of preribosome / ribosome assembly / cytosolic ribosome assembly / response to radiation / large ribosomal subunit / transferase activity / 5S rRNA binding / ribosomal large subunit assembly ...DnaA-L2 complex / negative regulation of DNA-templated DNA replication initiation / assembly of large subunit precursor of preribosome / ribosome assembly / cytosolic ribosome assembly / response to radiation / large ribosomal subunit / transferase activity / 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 / ribosome / structural constituent of ribosome / translation / ribonucleoprotein complex / response to antibiotic / mRNA binding / RNA binding / zinc ion binding / cytosol / cytoplasm Similarity search - Function | |||||||||||||||||||||||||||
Biological species | ![]() ![]() ![]() | |||||||||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 1.95 Å | |||||||||||||||||||||||||||
![]() | Pichkur, E.B. / Panteleev, P.V. / Konevega, A.L. | |||||||||||||||||||||||||||
Funding support | 1items
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![]() | ![]() Title: Rumicidins are a family of mammalian host-defense peptides plugging the 70S ribosome exit tunnel. Authors: Pavel V Panteleev / Eugene B Pichkur / Roman N Kruglikov / Alena Paleskava / Olga V Shulenina / Ilia A Bolosov / Ivan V Bogdanov / Victoria N Safronova / Sergey V Balandin / Valeriya I ...Authors: Pavel V Panteleev / Eugene B Pichkur / Roman N Kruglikov / Alena Paleskava / Olga V Shulenina / Ilia A Bolosov / Ivan V Bogdanov / Victoria N Safronova / Sergey V Balandin / Valeriya I Marina / Tatiana I Kombarova / Olga V Korobova / Olga V Shamova / Alexander G Myasnikov / Alexander I Borzilov / Ilya A Osterman / Petr V Sergiev / Alexey A Bogdanov / Olga A Dontsova / Andrey L Konevega / Tatiana V Ovchinnikova / ![]() Abstract: The antimicrobial resistance crisis along with challenges of antimicrobial discovery revealed the vital necessity to develop new antibiotics. Many of the animal proline-rich antimicrobial peptides ...The antimicrobial resistance crisis along with challenges of antimicrobial discovery revealed the vital necessity to develop new antibiotics. Many of the animal proline-rich antimicrobial peptides (PrAMPs) inhibit the process of bacterial translation. Genome projects allowed to identify immune-related genes encoding animal host defense peptides. Here, using genome mining approach, we discovered a family of proline-rich cathelicidins, named rumicidins. The genes encoding these peptides are widespread among ruminant mammals. Biochemical studies indicated that rumicidins effectively inhibited the elongation stage of bacterial translation. The cryo-EM structure of the Escherichia coli 70S ribosome in complex with one of the representatives of the family revealed that the binding site of rumicidins span the ribosomal A-site cleft and the nascent peptide exit tunnel interacting with its constriction point by the conservative Trp23-Phe24 dyad. Bacterial resistance to rumicidins is mediated by knockout of the SbmA transporter or modification of the MacAB-TolC efflux pump. A wide spectrum of antibacterial activity, a high efficacy in the animal infection model, and lack of adverse effects towards human cells in vitro make rumicidins promising molecular scaffolds for development of ribosome-targeting antibiotics. | |||||||||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 2.3 MB | Display | ![]() |
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PDB format | ![]() | 1.8 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 46632MC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
+50S ribosomal protein ... , 21 types, 21 molecules 01BCFGHIJLMfhjlnoqrwy
-RNA chain , 2 types, 2 molecules DE
#5: RNA chain | Mass: 885064.500 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#6: RNA chain | Mass: 38483.926 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Large ribosomal subunit protein ... , 7 types, 7 molecules Kgiptux
#12: Protein | Mass: 10546.472 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#16: Protein | Mass: 18801.598 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#18: Protein | Mass: 16050.606 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#23: Protein | Mass: 13396.828 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#26: Protein | Mass: 11078.874 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#27: Protein | Mass: 10713.465 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#29: Protein | Mass: 7155.267 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Protein/peptide , 1 types, 1 molecules T
#31: Protein/peptide | Mass: 2008.397 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Non-polymers , 5 types, 4607 molecules 








#32: Chemical | ChemComp-ZN / | ||||||
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#33: Chemical | ChemComp-MG / #34: Chemical | ChemComp-K / #35: Chemical | ChemComp-MS6 / ( | #36: Water | ChemComp-HOH / | |
-Details
Has ligand of interest | N |
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Has protein modification | Y |
-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: E. coli 70S ribosome in complex with PrAMP rumicidin-2 Type: RIBOSOME / Entity ID: #1-#31 / Source: MULTIPLE SOURCES |
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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 | 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: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 20000 nm / Nominal defocus min: 500 nm / Cs: 0.1 mm / C2 aperture diameter: 100 µm |
Image recording | Electron dose: 80 e/Å2 / Detector mode: INTEGRATING / Film or detector model: FEI FALCON II (4k x 4k) |
Image scans | Movie frames/image: 32 |
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Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||
3D reconstruction | Resolution: 1.95 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 371000 / Symmetry type: POINT | ||||||||||||||||||||
Atomic model building | Protocol: OTHER | ||||||||||||||||||||
Atomic model building | PDB-ID: 8B0X Accession code: 8B0X / Source name: PDB / Type: experimental model |