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Structural basis of dcp2 recognition and activation by dcp1.
- Source :
-
Molecular cell [Mol Cell] 2008 Feb 15; Vol. 29 (3), pp. 337-49. - Publication Year :
- 2008
-
Abstract
- A critical step in mRNA degradation is the removal of the 5' cap structure, which is catalyzed by the Dcp1-Dcp2 complex. The crystal structure of an S. pombe Dcp1p-Dcp2n complex combined with small-angle X-ray scattering analysis (SAXS) reveals that Dcp2p exists in open and closed conformations, with the closed complex being, or closely resembling, the catalytically more active form. This suggests that a conformational change between these open and closed complexes might control decapping. A bipartite RNA-binding channel containing the catalytic site and Box B motif is identified with a bound ATP located in the catalytic pocket in the closed complex, suggesting possible interactions that facilitate substrate binding. Dcp1 stimulates the activity of Dcp2 by promoting and/or stabilizing the closed complex. Notably, the interface of Dcp1 and Dcp2 is not fully conserved, explaining why the Dcp1-Dcp2 interaction in higher eukaryotes requires an additional factor.
- Subjects :
- Adenosine Triphosphate chemistry
Alanine metabolism
Amino Acid Motifs
Amino Acid Sequence
Amino Acid Substitution
Base Sequence
Binding Sites
Crystallography, X-Ray
Glutathione Transferase metabolism
Models, Molecular
Molecular Sequence Data
Protein Binding
Protein Structure, Quaternary
Protein Structure, Secondary
Protein Structure, Tertiary
Recombinant Fusion Proteins chemistry
Recombinant Fusion Proteins metabolism
Schizosaccharomyces pombe Proteins genetics
Structural Homology, Protein
Schizosaccharomyces pombe Proteins chemistry
Schizosaccharomyces pombe Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1097-2765
- Volume :
- 29
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Molecular cell
- Publication Type :
- Academic Journal
- Accession number :
- 18280239
- Full Text :
- https://doi.org/10.1016/j.molcel.2008.01.002