Structural basis of dcp2 recognition and activation by dcp1

She, M.; Svergun, D. I.; Decker, C. J.; Chen, N.; Round, A.; Song, H.; Muhlrad, D.; Parker, R.

doi:10.1016/j.molcel.2008.01.002

Journal Article

Structural basis of dcp2 recognition and activation by dcp1

She, M. ; Decker, C. J. ; Svergun, D. I. ; Round, A. ; Chen, N. ; Muhlrad, D. ; Parker, R. ; Song, H. ; DESY

2008
Cell Press [Cambridge, Mass.]

Molecular cell 29, 337-349 (2008) [10.1016/j.molcel.2008.01.002]

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Please use a persistent id in citations: doi:10.1016/j.molcel.2008.01.002

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.

Keyword(s): Adenosine Triphosphate: chemistry (MeSH) ; Alanine: metabolism (MeSH) ; Amino Acid Motifs (MeSH) ; Amino Acid Sequence (MeSH) ; Amino Acid Substitution (MeSH) ; Base Sequence (MeSH) ; Binding Sites (MeSH) ; Crystallography, X-Ray (MeSH) ; Glutathione Transferase: metabolism (MeSH) ; Models, Molecular (MeSH) ; Molecular Sequence Data (MeSH) ; Protein Binding (MeSH) ; Protein Structure, Quaternary (MeSH) ; Protein Structure, Secondary (MeSH) ; Protein Structure, Tertiary (MeSH) ; Recombinant Fusion Proteins: chemistry (MeSH) ; Recombinant Fusion Proteins: metabolism (MeSH) ; Schizosaccharomyces pombe Proteins: chemistry (MeSH) ; Schizosaccharomyces pombe Proteins: genetics (MeSH) ; Schizosaccharomyces pombe Proteins: metabolism (MeSH) ; Structural Homology, Protein (MeSH) ; Dcp1 protein, S pombe ; Dcp2 protein, S pombe ; Recombinant Fusion Proteins ; Schizosaccharomyces pombe Proteins ; Alanine ; Adenosine Triphosphate ; Glutathione Transferase