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Yorodumi- PDB-5fdv: Crystal structure of the Pyrrhocoricin antimicrobial peptide boun... -
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Basic information
| Entry | Database: PDB / ID: 5fdv | ||||||
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| Title | Crystal structure of the Pyrrhocoricin antimicrobial peptide bound to the Thermus thermophilus 70S ribosome | ||||||
Components |
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Keywords | RIBOSOME / bacterial ribosome / proline-rich antimicrobial peptide / antibiotics / protein biosynthesis | ||||||
| Function / homology | Function and homology informationdormancy process / negative regulation of translational elongation / ribosomal small subunit binding / negative regulation of translational initiation / response to cold / large ribosomal subunit / transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit ...dormancy process / negative regulation of translational elongation / ribosomal small subunit binding / negative regulation of translational initiation / response to cold / large ribosomal subunit / transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / defense response to bacterium / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / innate immune response / mRNA binding / extracellular region / zinc ion binding / metal ion binding / cytoplasm / cytosol Similarity search - Function | ||||||
| Biological species | ![]() Thermus thermophilus HB8 (bacteria)![]() Pyrrhocoris apterus (insect) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å | ||||||
Authors | Seefeldt, A.C. / Graf, M. / Perebaskine, N. / Nguyen, F. / Arenz, S. / Mardirossian, M. / Scocchi, M. / Wilson, D.N. / Innis, C.A. | ||||||
Citation | Journal: Nucleic Acids Res. / Year: 2016Title: Structure of the mammalian antimicrobial peptide Bac7(1-16) bound within the exit tunnel of a bacterial ribosome. Authors: Seefeldt, A.C. / Graf, M. / Perebaskine, N. / Nguyen, F. / Arenz, S. / Mardirossian, M. / Scocchi, M. / Wilson, D.N. / Innis, C.A. | ||||||
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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 | 5fdv.cif.gz | 7.6 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb5fdv.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 5fdv.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 5fdv_validation.pdf.gz | 1.9 MB | Display | wwPDB validaton report |
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| Full document | 5fdv_full_validation.pdf.gz | 3 MB | Display | |
| Data in XML | 5fdv_validation.xml.gz | 747.5 KB | Display | |
| Data in CIF | 5fdv_validation.cif.gz | 1.1 MB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fd/5fdv ftp://data.pdbj.org/pub/pdb/validation_reports/fd/5fdv | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 5f8kC ![]() 5fduC ![]() 4y4oS S: Starting model for refinement C: citing same article ( |
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| Similar structure data |
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Assembly
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Components
-RNA chain , 3 types, 6 molecules 1A2A1B2B1a2a
| #1: RNA chain | Mass: 948007.562 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() Thermus thermophilus HB8 (bacteria) / References: GenBank: 55771382#2: RNA chain | Mass: 38882.207 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() Thermus thermophilus HB8 (bacteria) / References: GenBank: 55771382#32: RNA chain | Mass: 493863.625 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() Thermus thermophilus HB8 (bacteria) / References: GenBank: 55771382 |
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+50S ribosomal protein ... , 29 types, 58 molecules 1D2D1E2E1F2F1G2G1H2H1I2I1N2N1O2O1P2P1Q2Q1R2R1S2S1T2T1U2U1V2V...
-30S ribosomal protein ... , 20 types, 40 molecules 1b2b1c2c1d2d1e2e1f2f1g2g1h2h1i2i1j2j1k2k1l2l1m2m1n2n1o2o1p2p...
| #34: Protein | Mass: 26646.852 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() Thermus thermophilus HB8 (bacteria) / References: UniProt: P80371#35: Protein | Mass: 22862.430 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() Thermus thermophilus HB8 (bacteria) / References: UniProt: P80372#36: Protein | Mass: 24242.254 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() Thermus thermophilus HB8 (bacteria) / References: UniProt: P80373#37: Protein | Mass: 16144.848 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() Thermus thermophilus HB8 (bacteria) / References: UniProt: Q5SHQ5#38: Protein | Mass: 11917.675 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() Thermus thermophilus HB8 (bacteria) / References: UniProt: Q5SLP8#39: Protein | Mass: 17919.775 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() Thermus thermophilus HB8 (bacteria) / References: UniProt: P17291#40: Protein | Mass: 15737.372 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() Thermus thermophilus HB8 (bacteria) / References: UniProt: Q5SHQ2, UniProt: A0A0M9AFS9*PLUS#41: Protein | Mass: 14279.419 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() Thermus thermophilus HB8 (bacteria) / References: UniProt: P80374#42: Protein | Mass: 11169.997 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() Thermus thermophilus HB8 (bacteria) / References: UniProt: Q5SHN7#43: Protein | Mass: 12032.662 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() Thermus thermophilus HB8 (bacteria) / References: UniProt: P80376#44: Protein | Mass: 13650.211 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() Thermus thermophilus HB8 (bacteria) / References: UniProt: Q5SHN3#45: Protein | Mass: 13237.430 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() Thermus thermophilus HB8 (bacteria) / References: UniProt: P80377#46: Protein | Mass: 7027.529 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() Thermus thermophilus HB8 (bacteria) / References: UniProt: Q5SHQ1, UniProt: A0A0N0BLP2*PLUS#47: Protein | Mass: 10447.213 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() Thermus thermophilus HB8 (bacteria) / References: UniProt: Q5SJ76#48: Protein | Mass: 9795.354 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() Thermus thermophilus HB8 (bacteria) / References: UniProt: Q5SJH3#49: Protein | Mass: 11722.904 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() Thermus thermophilus HB8 (bacteria) / References: UniProt: Q5SHP7, UniProt: A0A0N0BLS5*PLUS#50: Protein | Mass: 7897.451 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() Thermus thermophilus HB8 (bacteria) / References: UniProt: Q5SLQ0#51: Protein | Mass: 9455.995 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() Thermus thermophilus HB8 (bacteria) / References: UniProt: Q5SHP2#52: Protein | Mass: 10876.067 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() Thermus thermophilus HB8 (bacteria) / References: UniProt: P80380#53: Protein/peptide | Mass: 2831.295 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Thermus thermophilus HB8 (bacteria) / Gene: rpsU, TTHA1396 / Plasmid: pGS21a / Production host: ![]() |
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-Protein / Protein/peptide , 2 types, 4 molecules 2x1x1y2y
| #33: Protein | Mass: 10964.620 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: cell / Source: (natural) ![]() #54: Protein/peptide | Mass: 1796.098 Da / Num. of mol.: 2 / Fragment: UNP residues 1-16 / Source method: obtained synthetically / Details: chemical synthesis / Source: (synth.) Pyrrhocoris apterus (insect) / References: UniProt: P37362 |
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-Non-polymers , 5 types, 6981 molecules 








| #55: Chemical | ChemComp-MG / #56: Chemical | ChemComp-ZN / #57: Chemical | #58: Chemical | ChemComp-A / | #59: Water | ChemComp-HOH / | |
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-Details
| Has protein modification | Y |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 3.42 Å3/Da / Density % sol: 63.99 % |
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| Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.6 / Details: Tris-HCl, PEG 20000, MPD, Arginine |
-Data collection
| Diffraction | Mean temperature: 100 K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Diffraction source | Source: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 1 / Wavelength: 0.987 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Dec 4, 2015 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Radiation wavelength | Wavelength: 0.987 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Reflection | Resolution: 2.8→50 Å / Num. obs: 1428776 / % possible obs: 100 % / Observed criterion σ(I): -3 / Redundancy: 13.8 % / Biso Wilson estimate: 64.57 Å2 / Rmerge F obs: 0.999 / Rmerge(I) obs: 0.172 / Rrim(I) all: 0.178 / Χ2: 0.967 / Net I/σ(I): 15.99 / Num. measured all: 19712065 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Reflection shell | Diffraction-ID: 1 / Rejects: _
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 4Y4O Resolution: 2.8→49.812 Å / FOM work R set: 0.8317 / SU ML: 0.39 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 24.43 / Stereochemistry target values: ML
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| Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso max: 149.28 Å2 / Biso mean: 60.09 Å2 / Biso min: 8.77 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: final / Resolution: 2.8→49.812 Å
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| Refine LS restraints |
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| LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 30 / % reflection obs: 100 %
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Thermus thermophilus HB8 (bacteria)
Pyrrhocoris apterus (insect)
X-RAY DIFFRACTION
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