[English] 日本語
Yorodumi- PDB-4ifd: Crystal structure of an 11-subunit eukaryotic exosome complex bou... -
+
Open data
-
Basic information
| Entry | Database: PDB / ID: 4ifd | ||||||
|---|---|---|---|---|---|---|---|
| Title | Crystal structure of an 11-subunit eukaryotic exosome complex bound to RNA | ||||||
Components |
| ||||||
Keywords | HYDROLASE/RNA / EXOSOME / RNA / RRP44 / DIS3 / PIN / RRP6 / EXONUCLEASE / ENDONUCLEASE / HYDROLASE / NUCLEASE / RIBONUCLEASE / RNA PROCESSING / HYDROLASE-RNA complex | ||||||
| Function / homology | Function and homology informationnuclear polyadenylation-dependent antisense transcript catabolic process / nuclear polyadenylation-dependent snoRNA catabolic process / nuclear polyadenylation-dependent snRNA catabolic process / mRNA decay by 3' to 5' exoribonuclease / Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA / Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA / nuclear polyadenylation-dependent mRNA catabolic process / nuclear mRNA surveillance of mRNA 3'-end processing / regulatory ncRNA 3'-end processing / U1 snRNA 3'-end processing ...nuclear polyadenylation-dependent antisense transcript catabolic process / nuclear polyadenylation-dependent snoRNA catabolic process / nuclear polyadenylation-dependent snRNA catabolic process / mRNA decay by 3' to 5' exoribonuclease / Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA / Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA / nuclear polyadenylation-dependent mRNA catabolic process / nuclear mRNA surveillance of mRNA 3'-end processing / regulatory ncRNA 3'-end processing / U1 snRNA 3'-end processing / nuclear polyadenylation-dependent CUT catabolic process / U5 snRNA 3'-end processing / TRAMP-dependent tRNA surveillance pathway / exosome (RNase complex) / CUT catabolic process / cytoplasmic exosome (RNase complex) / U4 snRNA 3'-end processing / nuclear polyadenylation-dependent rRNA catabolic process / poly(A)-dependent snoRNA 3'-end processing / nuclear-transcribed mRNA catabolic process, non-stop decay / nuclear exosome (RNase complex) / nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay / exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / histone mRNA catabolic process / nuclear mRNA surveillance / post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery / rRNA catabolic process / rRNA primary transcript binding / mRNA 3'-UTR AU-rich region binding / Hydrolases; Acting on ester bonds; Endoribonucleases producing 5'-phosphomonoesters / RNA catabolic process / regulation of telomere maintenance / nonfunctional rRNA decay / Major pathway of rRNA processing in the nucleolus and cytosol / rRNA metabolic process / mRNA catabolic process / nuclear-transcribed mRNA catabolic process / RNA processing / RNA endonuclease activity / mRNA processing / manganese ion binding / Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters / 3'-5'-RNA exonuclease activity / endonuclease activity / tRNA binding / single-stranded RNA binding / nucleotide binding / nucleolus / mitochondrion / RNA binding / nucleoplasm / nucleus / cytoplasm Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.805 Å | ||||||
Authors | Makino, D.L. / Conti, E. | ||||||
Citation | Journal: Nature / Year: 2013Title: Crystal structure of an RNA-bound 11-subunit eukaryotic exosome complex. Authors: Makino, D.L. / Baumgartner, M. / Conti, E. | ||||||
| History |
|
-
Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
|---|
-
Downloads & links
-
Download
| PDBx/mmCIF format | 4ifd.cif.gz | 1.3 MB | Display | PDBx/mmCIF format |
|---|---|---|---|---|
| PDB format | pdb4ifd.ent.gz | 1.1 MB | Display | PDB format |
| PDBx/mmJSON format | 4ifd.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 4ifd_validation.pdf.gz | 576.2 KB | Display | wwPDB validaton report |
|---|---|---|---|---|
| Full document | 4ifd_full_validation.pdf.gz | 611.4 KB | Display | |
| Data in XML | 4ifd_validation.xml.gz | 114.3 KB | Display | |
| Data in CIF | 4ifd_validation.cif.gz | 157 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/if/4ifd ftp://data.pdbj.org/pub/pdb/validation_reports/if/4ifd | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
| Deposited unit | ![]()
| ||||||||
|---|---|---|---|---|---|---|---|---|---|
| 1 |
| ||||||||
| Unit cell |
|
-
Components
-Exosome complex component ... , 9 types, 9 molecules ABCDEFGHI
| #1: Protein | Mass: 33870.668 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 204508 / S288c / Gene: D9954.1, RRP45, YDR280W / Plasmid: pETMCN / Production host: ![]() |
|---|---|
| #2: Protein | Mass: 27794.926 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 204508 / S288c / Gene: ECM20, G7587, RRP41, SKI6, YGR195W / Plasmid: pETMCN / Production host: ![]() |
| #3: Protein | Mass: 43977.805 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 204508 / S288c / Gene: RRP43, YCR035C, YCR35C, YCR522 / Plasmid: pETMCN / Production host: ![]() |
| #4: Protein | Mass: 26913.988 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 204508 / S288c / Gene: RRP46, YGR095C / Plasmid: pETMCN / Production host: ![]() |
| #5: Protein | Mass: 29294.398 Da / Num. of mol.: 1 / Mutation: V138I Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 204508 / S288c / Gene: RRP42, YDL111C / Plasmid: pETMCN / Production host: ![]() |
| #6: Protein | Mass: 27559.869 Da / Num. of mol.: 1 / Mutation: T75S, M161T Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 204508 / S288c / Gene: G6676, MTR3, YGR158C / Plasmid: pETMCN / Production host: ![]() |
| #7: Protein | Mass: 26778.551 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 204508 / S288c / Gene: RRP40, YOL142W / Plasmid: pETMCN / Production host: ![]() |
| #8: Protein | Mass: 39714.445 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 204508 / S288c / Gene: RRP4, YHR069C / Plasmid: pECK / Production host: ![]() |
| #9: Protein | Mass: 32805.645 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 204508 / S288c / Gene: CSL4, N1154, SKI4, YNL232W / Plasmid: pETM13 / Production host: ![]() |
-Exosome complex exonuclease ... , 2 types, 2 molecules JK
| #10: Protein | Mass: 113983.898 Da / Num. of mol.: 1 / Mutation: D171N, D551N Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 204508 / S288c / Gene: DIS3, O2197, RRP44, YOL021C / Plasmid: pETM11 / Production host: ![]() References: UniProt: Q08162, Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters, Hydrolases; Acting on ester bonds; Endoribonucleases producing 5'-phosphomonoesters |
|---|---|
| #11: Protein | Mass: 19876.869 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 518-693 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 204508 / S288c / Gene: RRP6, UNC733, YOR001W / Plasmid: pECK / Production host: ![]() References: UniProt: Q12149, Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters |
-RNA chain , 1 types, 1 molecules R
| #12: RNA chain | Mass: 14046.938 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: Sequence designed based on biochemical data. |
|---|
-Non-polymers , 6 types, 262 molecules 










| #13: Chemical | ChemComp-BR / #14: Chemical | ChemComp-GOL / #15: Chemical | ChemComp-MES / | #16: Chemical | ChemComp-MG / | #17: Chemical | ChemComp-ZN / | #18: Water | ChemComp-HOH / | |
|---|
-Details
| Has protein modification | Y |
|---|
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 10 |
|---|
-
Sample preparation
| Crystal | Density Matthews: 2.67 Å3/Da / Density % sol: 53.93 % |
|---|---|
| Crystal grow | Temperature: 292 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 0.02M Tris pH7.5, 0.05M NaCl, 0.001M MnCl2, 0.002M MgCl2, 1mM TCEP, 0.15M MES pH6.5, 0.27M NaBr, 11.4-12.2% PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 292K |
-Data collection
| Diffraction | Mean temperature: 100 K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.9199 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Detector | Type: PSI PILATUS 6M / Detector: PIXEL / Date: Oct 28, 2011 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Radiation wavelength | Wavelength: 0.9199 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Reflection | Resolution: 2.805→49.64 Å / Num. all: 99137 / Num. obs: 99137 / % possible obs: 87.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 12.8 % / Biso Wilson estimate: 59.5 Å2 / Rmerge(I) obs: 0.176 / Net I/σ(I): 12.25 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Reflection shell |
|
-
Processing
| Software |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 2NN6, 2WP8, 2JA9, 2JE6 Resolution: 2.805→49.638 Å / SU ML: 0.36 / Cross valid method: THROUGHOUT / σ(F): 1.99 / Phase error: 24.2 / Stereochemistry target values: ML
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Solvent computation | Shrinkage radii: 1 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 2.805→49.638 Å
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refine LS restraints |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 30
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement TLS group |
|
Movie
Controller
About Yorodumi




X-RAY DIFFRACTION
Citation











PDBj





































