|Entry||Database: PDB / ID: 4a53|
|Title||Structural basis of the Dcp1:Dcp2 mRNA decapping complex activation by Edc3 and Scd6|
|Keywords||RNA BINDING PROTEIN|
|Function / homology|
Function and homology information
deadenylation-independent decapping of nuclear-transcribed mRNA / P-body assembly / P-body / cytoplasmic stress granule / mRNA binding / cytoplasm
Similarity search - Function
Lsm16, N-terminal / FDF domain / FDF domain / FDF / DFDF domain / DFDF domain profile. / YjeF-related protein N-terminus / YjeF N-terminal domain superfamily / YjeF N-terminal domain / YjeF N-terminal domain profile. ...Lsm16, N-terminal / FDF domain / FDF domain / FDF / DFDF domain / DFDF domain profile. / YjeF-related protein N-terminus / YjeF N-terminal domain superfamily / YjeF N-terminal domain / YjeF N-terminal domain profile. / SH3 type barrels. - #100 / SH3 type barrels. / Roll / Mainly Beta
Similarity search - Domain/homology
Enhancer of mRNA-decapping protein 3
Similarity search - Component
|Biological species||SCHIZOSACCHAROMYCES POMBE (fission yeast)|
|Method||SOLUTION NMR / XPLOR|
|Authors||Fromm, S.A. / Truffault, V. / Kamenz, J. / Braun, J.E. / Hoffmann, N.A. / Izaurralde, E. / Sprangers, R.|
|Citation||Journal: Embo J. / Year: 2011|
Title: The Structural Basis of Edc3- and Scd6-Mediated Activation of the Dcp1:Dcp2 Mrna Decapping Complex.
Authors: Fromm, S.A. / Truffault, V. / Kamenz, J. / Braun, J.E. / Hoffmann, N.A. / Izaurralde, E. / Sprangers, R.
|Structure viewer||Molecule: |
Downloads & links
|#1: Protein|| |
Mass: 14016.722 Da / Num. of mol.: 1 / Fragment: LSM, RESIDUES 1-121
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) SCHIZOSACCHAROMYCES POMBE (fission yeast)
Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / References: UniProt: O94752
|Experiment||Method: SOLUTION NMR|
|NMR experiment||Type: NOESY|
|NMR details||Text: NONE|
|Details||Contents: 90% WATER/10% D2O|
|Sample conditions||Ionic strength: 125 mM / pH: 7.3 / Pressure: 1.0 atm / Temperature: 303.0 K|
|NMR spectrometer||Type: Bruker Avance / Manufacturer: Bruker / Model: Avance / Field strength: 800 MHz|
|Refinement||Method: XPLOR / Software ordinal: 1|
|NMR ensemble||Conformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 50 / Conformers submitted total number: 20|
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