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Yorodumi- PDB-5lm5: Structure of C-terminal domain from S. cerevisiae Pat1 decapping ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5lm5 | ||||||
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Title | Structure of C-terminal domain from S. cerevisiae Pat1 decapping activator bound to Dcp2 HLM2 peptide (region 435-451) | ||||||
Components |
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Keywords | RNA BINDING PROTEIN / Protein peptide complex / ISOMERASE | ||||||
Function / homology | Function and homology information RNA decapping complex / Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA / Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA / deadenylation-independent decapping of nuclear-transcribed mRNA / mRNA 5'-diphosphatase activity / mRNA decay by 5' to 3' exoribonuclease / 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] hydrolase / Lsm1-7-Pat1 complex / 5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity / cytoplasmic side of membrane ...RNA decapping complex / Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA / Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA / deadenylation-independent decapping of nuclear-transcribed mRNA / mRNA 5'-diphosphatase activity / mRNA decay by 5' to 3' exoribonuclease / 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] hydrolase / Lsm1-7-Pat1 complex / 5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity / cytoplasmic side of membrane / deadenylation-dependent decapping of nuclear-transcribed mRNA / formation of translation preinitiation complex / P-body assembly / regulation of translational initiation / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / positive regulation of transcription initiation by RNA polymerase II / cellular response to glucose starvation / stress granule assembly / negative regulation of translational initiation / P-body / kinetochore / cytoplasmic stress granule / mRNA processing / manganese ion binding / cytosolic small ribosomal subunit / hydrolase activity / cell division / chromatin binding / mRNA binding / RNA binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.6 Å | ||||||
Authors | Charenton, C. / Gaudon-Plesse, C. / Fourati, Z. / Taverniti, V. / Back, R. / Kolesnikova, O. / Seraphin, B. / Graille, M. | ||||||
Citation | Journal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2017 Title: A unique surface on Pat1 C-terminal domain directly interacts with Dcp2 decapping enzyme and Xrn1 5'-3' mRNA exonuclease in yeast. Authors: Charenton, C. / Gaudon-Plesse, C. / Fourati, Z. / Taverniti, V. / Back, R. / Kolesnikova, O. / Seraphin, B. / Graille, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5lm5.cif.gz | 274.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5lm5.ent.gz | 223.7 KB | Display | PDB format |
PDBx/mmJSON format | 5lm5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5lm5_validation.pdf.gz | 456.7 KB | Display | wwPDB validaton report |
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Full document | 5lm5_full_validation.pdf.gz | 468.6 KB | Display | |
Data in XML | 5lm5_validation.xml.gz | 22.9 KB | Display | |
Data in CIF | 5lm5_validation.cif.gz | 30.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lm/5lm5 ftp://data.pdbj.org/pub/pdb/validation_reports/lm/5lm5 | HTTPS FTP |
-Related structure data
Related structure data | 5lmfC 5lmgC 4ogpS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 42282.438 Da / Num. of mol.: 2 / Mutation: Q706A/L713A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Gene: PAT1, MRT1, YCR077C, YCR77C / Production host: Escherichia coli (E. coli) / References: UniProt: P25644 #2: Protein/peptide | Mass: 1459.623 Da / Num. of mol.: 2 / Fragment: UNP residues 436-449 / Source method: obtained synthetically / Source: (synth.) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: B3LNX5, UniProt: P53550*PLUS |
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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: 2.29 Å3/Da / Density % sol: 46.35 % |
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Crystal grow | Temperature: 297.15 K / Method: vapor diffusion, hanging drop / Details: 0.2 M MgCl2 20%PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 1 / Wavelength: 0.97533 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Jul 3, 2014 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.97533 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.6→50 Å / Num. obs: 21634 / % possible obs: 99.1 % / Observed criterion σ(I): -3 / Redundancy: 4.3 % / Biso Wilson estimate: 83.16 Å2 / CC1/2: 0.996 / Rmerge(I) obs: 0.134 / Net I/σ(I): 6.52 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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-Phasing
Phasing | Method: molecular replacement |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 4OGP Resolution: 2.6→49.14 Å / Cor.coef. Fo:Fc: 0.909 / Cor.coef. Fo:Fc free: 0.916 / Rfactor Rfree error: 0 / SU R Cruickshank DPI: 2.926 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 1.725 / SU Rfree Blow DPI: 0.336 / SU Rfree Cruickshank DPI: 0.347
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Displacement parameters | Biso max: 199.74 Å2 / Biso mean: 108.91 Å2 / Biso min: 62.13 Å2
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Refine analyze | Luzzati coordinate error obs: 1.03 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.6→49.14 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.6→2.73 Å / Total num. of bins used: 11
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Refinement TLS params. | T22: 0.6079 Å2 / Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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