|Entry||Database: PDB / ID: 1whv|
|Title||Solution structure of the RNA binding domain from hypothetical protein BAB23382|
|Components||poly(A)-specific ribonucleasePoly(A)-specific ribonuclease|
|Keywords||HYDROLASE / RNA recognition motif / RRM / RNA binding domain / RBD / RNP / poly(A)-specific ribonuclease / PARN / STRUCTURAL GENOMICS / RIKEN Structural Genomics/Proteomics Initiative / RSGI|
|Function / homology|
Function and homology information
KSRP (KHSRP) binds and destabilizes mRNA / ncRNA deadenylation / box H/ACA RNA 3'-end processing / Deadenylation of mRNA / miRNA catabolic process / poly(A)-specific ribonuclease / telomerase RNA stabilization / cation binding / poly(A)-specific ribonuclease activity / regulation of telomerase RNA localization to Cajal body ...KSRP (KHSRP) binds and destabilizes mRNA / ncRNA deadenylation / box H/ACA RNA 3'-end processing / Deadenylation of mRNA / miRNA catabolic process / poly(A)-specific ribonuclease / telomerase RNA stabilization / cation binding / poly(A)-specific ribonuclease activity / regulation of telomerase RNA localization to Cajal body / polyadenylation-dependent snoRNA 3'-end processing / nuclear-transcribed mRNA poly(A) tail shortening / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / positive regulation of telomere maintenance via telomerase / positive regulation of telomerase activity / RNA phosphodiester bond hydrolysis, exonucleolytic / 3'-5'-exoribonuclease activity / nuclear speck / nucleolus / protein kinase binding / RNA binding / metal ion binding / cytoplasm
Similarity search - Function
PARN, R3H domain / RNA binding domain / Poly(A)-specific ribonuclease, RNA-binding / R3H domain / Ribonuclease CAF1 / CAF1 family ribonuclease / R3H domain profile. / R3H domain superfamily / R3H domain / RRM (RNA recognition motif) domain ...PARN, R3H domain / RNA binding domain / Poly(A)-specific ribonuclease, RNA-binding / R3H domain / Ribonuclease CAF1 / CAF1 family ribonuclease / R3H domain profile. / R3H domain superfamily / R3H domain / RRM (RNA recognition motif) domain / RNA-binding domain superfamily / Ribonuclease H superfamily / Ribonuclease H-like superfamily / Nucleotide-binding alpha-beta plait domain superfamily / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Poly(A)-specific ribonuclease PARN
Similarity search - Component
|Biological species||Mus musculus (house mouse)|
|Method||SOLUTION NMR / torsion angle dynamics, simulated annealing|
|Authors||Nagata, T. / Muto, Y. / Inoue, M. / Kigawa, T. / Terada, T. / Shirouzu, M. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI)|
|Citation||Journal: To be Published|
Title: Solution structure of the RNA binding domain from hypothetical protein BAB23382
Authors: Nagata, T. / Muto, Y. / Inoue, M. / Kigawa, T. / Terada, T. / Shirouzu, M. / Yokoyama, S.
|Structure viewer||Molecule: |
Downloads & links
A: poly(A)-specific ribonuclease
|#1: Protein|| |
Mass: 11013.168 Da / Num. of mol.: 1 / Fragment: RNA recognition motif
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Description: CELL-FREE PROTEIN SYNTHESIS / Gene: RIKEN CDNA 1200003I18 / Plasmid: P031020-39 / References: UniProt: Q8VDG3
|Experiment||Method: SOLUTION NMR|
|NMR details||Text: The structure was determined using triple-resonance NMR spectroscopy.|
|Details||Contents: 0.94mM PROTEIN U-15N, 13C; 20mM phosphate buffer NA; 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O; 10% D2O|
Solvent system: 90% H2O/10% D2O
|Sample conditions||Ionic strength: 100mM / pH: 6.0 / Pressure: ambient / Temperature: 298 K|
|Radiation||Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M|
|Radiation wavelength||Relative weight: 1|
|NMR spectrometer||Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz|
|Refinement||Method: torsion angle dynamics, simulated annealing / 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|
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