+Open data
-Basic information
Entry | Database: PDB / ID: 7qy5 | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal structure of the S.pombe Ars2-Red1 complex. | ||||||
Components |
| ||||||
Keywords | RNA / RNA degradation / RNA targeting complex | ||||||
Function / homology | Function and homology information MTREC complex / regulatory ncRNA-mediated heterochromatin formation / mRNA processing / nuclear body / chromatin / nucleus / metal ion binding Similarity search - Function | ||||||
Biological species | Schizosaccharomyces pombe (fission yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.77 Å | ||||||
Authors | Foucher, A.E. / Kadlec, J. | ||||||
Funding support | France, 1items
| ||||||
Citation | Journal: Nat Commun / Year: 2022 Title: Structural analysis of Red1 as a conserved scaffold of the RNA-targeting MTREC/PAXT complex. Authors: Foucher, A.E. / Touat-Todeschini, L. / Juarez-Martinez, A.B. / Rakitch, A. / Laroussi, H. / Karczewski, C. / Acajjaoui, S. / Soler-Lopez, M. / Cusack, S. / Mackereth, C.D. / Verdel, A. / Kadlec, J. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 7qy5.cif.gz | 189.7 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb7qy5.ent.gz | 149.2 KB | Display | PDB format |
PDBx/mmJSON format | 7qy5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7qy5_validation.pdf.gz | 473.2 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 7qy5_full_validation.pdf.gz | 480.9 KB | Display | |
Data in XML | 7qy5_validation.xml.gz | 30.2 KB | Display | |
Data in CIF | 7qy5_validation.cif.gz | 41.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qy/7qy5 ftp://data.pdbj.org/pub/pdb/validation_reports/qy/7qy5 | HTTPS FTP |
-Related structure data
Related structure data | 7quuC C: citing same article (ref.) |
---|---|
Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 14315.451 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Schizosaccharomyces pombe (fission yeast) Strain: 972 / ATCC 24843 / Gene: pir2, ars2, SPBC725.08 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Star / References: UniProt: O94326 #2: Protein/peptide | Mass: 2401.233 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) Schizosaccharomyces pombe (fission yeast) #3: Protein | Mass: 38815.859 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Schizosaccharomyces pombe (fission yeast) Strain: 972 / ATCC 24843 / Gene: pir2, ars2, SPBC725.08 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Star / References: UniProt: O94326 #4: Chemical | Has ligand of interest | N | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 3.46 Å3/Da / Density % sol: 64.41 % |
---|---|
Crystal grow | Temperature: 278.15 K / Method: vapor diffusion, sitting drop / pH: 8 / Details: 200mM Ammonium Formate, 20% PEG3350 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID30B / Wavelength: 0.9677 Å |
Detector | Type: DECTRIS EIGER R 4M / Detector: PIXEL / Date: Nov 7, 2021 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9677 Å / Relative weight: 1 |
Reflection | Resolution: 2.77→84.85 Å / Num. obs: 26786 / % possible obs: 76 % / Redundancy: 5.56 % / CC1/2: 0.98 / Rmerge(I) obs: 0.29 / Net I/σ(I): 5.3 |
Reflection shell | Resolution: 2.771→2.994 Å / Redundancy: 6.2 % / Mean I/σ(I) obs: 1.5 / Num. unique obs: 1339 / CC1/2: 0.55 / % possible all: 18.4 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: alpafold Resolution: 2.77→84.85 Å / Cor.coef. Fo:Fc: 0.927 / Cor.coef. Fo:Fc free: 0.865 / SU B: 21.803 / SU ML: 0.401 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.488 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 160.83 Å2 / Biso mean: 52.291 Å2 / Biso min: 24 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.77→84.85 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.771→2.843 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
|