+Open data
-Basic information
Entry | Database: PDB / ID: 2rqh | ||||||
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Title | Structure of GSPT1/ERF3A-PABC | ||||||
Components |
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Keywords | PROTEIN BINDING / PROTEIN-PROTEIN COMPLEX / GTP-binding / Nucleotide-binding / Alternative splicing / Cytoplasm / Methylation / mRNA processing / mRNA splicing / Nucleus / Phosphoprotein / RNA-binding / Spliceosome | ||||||
Function / homology | Function and homology information Eukaryotic Translation Termination / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / mCRD-mediated mRNA stability complex / translation activator activity / translation release factor complex / negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / CRD-mediated mRNA stabilization / regulation of translational termination ...Eukaryotic Translation Termination / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / mCRD-mediated mRNA stability complex / translation activator activity / translation release factor complex / negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / CRD-mediated mRNA stabilization / regulation of translational termination / translation release factor activity / Z-decay: degradation of maternal mRNAs by zygotically expressed factors / Deadenylation of mRNA / positive regulation of cytoplasmic translation / mRNA stabilization / poly(A) binding / M-decay: degradation of maternal mRNAs by maternally stored factors / regulatory ncRNA-mediated gene silencing / poly(U) RNA binding / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / positive regulation of nuclear-transcribed mRNA poly(A) tail shortening / Translation initiation complex formation / : / cell leading edge / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / L13a-mediated translational silencing of Ceruloplasmin expression / positive regulation of viral genome replication / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / translational termination / catalytic step 2 spliceosome / cytosolic ribosome / mRNA 3'-UTR binding / AUF1 (hnRNP D0) binds and destabilizes mRNA / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / cytoplasmic ribonucleoprotein granule / mRNA splicing, via spliceosome / Regulation of expression of SLITs and ROBOs / cytoplasmic stress granule / lamellipodium / translation / ribonucleoprotein complex / focal adhesion / mRNA binding / GTPase activity / GTP binding / RNA binding / extracellular exosome / membrane / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Osawa, M. / Nakanishi, T. / Hosoda, N. / Uchida, S. / Hoshino, T. / Katada, I. / Shimada, I. | ||||||
Citation | Journal: To be Published Title: Eukaryotic Translation Termination Factor Gspt/Erf3 Recognizes Pabp with Chemical Exchange Using Two Overlapping Motifs Authors: Osawa, M. / Nakanishi, T. / Hosoda, N. / Uchida, S. / Hoshino, T. / Katada, I. / Shimada, I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2rqh.cif.gz | 616.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2rqh.ent.gz | 537 KB | Display | PDB format |
PDBx/mmJSON format | 2rqh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rq/2rqh ftp://data.pdbj.org/pub/pdb/validation_reports/rq/2rqh | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 2354.724 Da / Num. of mol.: 1 / Fragment: RESIDUES 73-94 (UNP residues 24-45) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Gspt1 / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q8K2E1, UniProt: Q8R050*PLUS |
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#2: Protein | Mass: 8996.363 Da / Num. of mol.: 1 / Fragment: PABC DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PABPC1, PAB1, PABP1, PABPC2 / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P11940 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1 mM G1 TO S PHASE TRANSITION 1-1, 1 mM [U-98% 13C; U-98% 15N] POLYADENYLATE-BINDING PROTEIN 1-2, 93% H2O/7% D2O Solvent system: 93% H2O/7% D2O | ||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0.15M / pH: 6.5 / Pressure: AMBIENT / Temperature: 303 K |
-NMR measurement
NMR spectrometer | Type: BRUKER AVANCE / Manufacturer: Bruker / Model: Avance / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 / Representative conformer: 1 |