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Open data
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Basic information
| Entry | Database: PDB / ID: 6f4a | ||||||
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| Title | Yeast mitochondrial RNA degradosome complex mtEXO | ||||||
Components |
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Keywords | HYDROLASE / RNA degradation / mitochondria / nuclease / helicase / protein complex | ||||||
| Function / homology | Function and homology informationmitochondrial degradosome / hydrolase activity, acting on acid anhydrides / exoribonuclease II activity / mitochondrial RNA catabolic process / mitochondrial chromosome / mitochondrial DNA replication / mRNA catabolic process / Group I intron splicing / RNA nuclease activity / P-body ...mitochondrial degradosome / hydrolase activity, acting on acid anhydrides / exoribonuclease II activity / mitochondrial RNA catabolic process / mitochondrial chromosome / mitochondrial DNA replication / mRNA catabolic process / Group I intron splicing / RNA nuclease activity / P-body / RNA helicase activity / RNA helicase / mitochondrion / RNA binding / ATP binding / metal ion binding Similarity search - Function | ||||||
| Biological species | Candida glabrata (fungus)![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.55 Å | ||||||
Authors | Razew, M. / Nowak, E. / Nowotny, M. | ||||||
| Funding support | Poland, 1items
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Citation | Journal: Nat Commun / Year: 2018Title: Structural analysis of mtEXO mitochondrial RNA degradosome reveals tight coupling of nuclease and helicase components. Authors: Razew, M. / Warkocki, Z. / Taube, M. / Kolondra, A. / Czarnocki-Cieciura, M. / Nowak, E. / Labedzka-Dmoch, K. / Kawinska, A. / Piatkowski, J. / Golik, P. / Kozak, M. / Dziembowski, A. / Nowotny, M. | ||||||
| History |
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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 | 6f4a.cif.gz | 434.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb6f4a.ent.gz | 338.1 KB | Display | PDB format |
| PDBx/mmJSON format | 6f4a.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 6f4a_validation.pdf.gz | 463.6 KB | Display | wwPDB validaton report |
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| Full document | 6f4a_full_validation.pdf.gz | 474.4 KB | Display | |
| Data in XML | 6f4a_validation.xml.gz | 39.3 KB | Display | |
| Data in CIF | 6f4a_validation.cif.gz | 55.2 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f4/6f4a ftp://data.pdbj.org/pub/pdb/validation_reports/f4/6f4a | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 6f3hSC ![]() 3rc3S S: Starting model for refinement C: citing same article ( |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| Unit cell |
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Components
| #1: Protein | Mass: 94687.203 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: 69 aminoacid N-terminal truncation was introduced in the full length protein Source: (gene. exp.) Candida glabrata (fungus) / Gene: AO440_004157 / Production host: ![]() |
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| #2: Protein | Mass: 73477.531 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: 42 aminoacid N-terminal truncation and 14 aminoacid C-terminal truncation was introduced to the full length protein Source: (gene. exp.) Candida glabrata (fungus) / Gene: SUV3, CAGL0L12386g / Production host: ![]() |
| #3: RNA chain | Mass: 1899.213 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: RNA molecule co-purified with the protein / Source: (natural) ![]() |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 3.3 Å3/Da / Density % sol: 62.76 % |
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| Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop Details: 0.2M ammonium citrate tribasic (pH 7.0), 18% (w/v) PEG3350 |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.97625 Å |
| Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: May 8, 2015 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.97625 Å / Relative weight: 1 |
| Reflection | Resolution: 3.55→50.1 Å / Num. obs: 26391 / % possible obs: 95.4 % / Redundancy: 4.3 % / Rrim(I) all: 0.033 / Net I/σ(I): 27.4 |
| Reflection shell | Resolution: 3.55→3.64 Å / Rrim(I) all: 0.225 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 6F3H, 3RC3 Resolution: 3.55→49.061 Å / SU ML: 0.53 / Cross valid method: FREE R-VALUE / σ(F): 1.38 / Phase error: 37.64 / Stereochemistry target values: MLHL
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| Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 3.55→49.061 Å
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| Refine LS restraints |
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| LS refinement shell |
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| Refinement TLS params. | Method: refined / Origin x: -3.4509 Å / Origin y: -51.2107 Å / Origin z: 31.8815 Å
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| Refinement TLS group | Selection details: all |
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About Yorodumi




Candida glabrata (fungus)
X-RAY DIFFRACTION
Poland, 1items
Citation









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