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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 | ||||||
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![]() | HYDROLASE / RNA degradation / mitochondria / nuclease / helicase / protein complex | ||||||
Function / homology | ![]() mitochondrial chromosome / mitochondrial degradosome / mitochondrial RNA catabolic process / exoribonuclease II activity / mitochondrial DNA replication / Group I intron splicing / RNA nuclease activity / RNA helicase activity / RNA helicase / mitochondrion ...mitochondrial chromosome / mitochondrial degradosome / mitochondrial RNA catabolic process / exoribonuclease II activity / mitochondrial DNA replication / Group I intron splicing / RNA nuclease activity / RNA helicase activity / RNA helicase / mitochondrion / RNA binding / ATP binding Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Razew, M. / Nowak, E. / Nowotny, M. | ||||||
Funding support | ![]()
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![]() | ![]() Title: 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 434.4 KB | Display | ![]() |
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PDB format | ![]() | 338.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 463.6 KB | Display | ![]() |
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Full document | ![]() | 474.4 KB | Display | |
Data in XML | ![]() | 39.3 KB | Display | |
Data in CIF | ![]() | 55.2 KB | Display | |
Arichive directory | ![]() ![]() | 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.) ![]() ![]() ![]() |
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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.) ![]() ![]() ![]() |
#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: ![]() |
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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: ![]() ![]() ![]() |
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: ![]() Starting 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 |