Structural Basis of Dcp2 Recognition and Activation by Dcp1

Autor: Meipei She, Carolyn J. Decker, Denise Muhlrad, Haiwei Song, Nan Chen, Dmitri I. Svergun, Roy Parker, Adam Round
Rok vydání: 2008
Předmět:
Models
Molecular
metabolism [Recombinant Fusion Proteins]
Conformational change
metabolism [Glutathione Transferase]
Stereochemistry
Recombinant Fusion Proteins
Amino Acid Motifs
Molecular Sequence Data
chemistry [Adenosine Triphosphate]
Dcp2 protein
S pombe
Plasma protein binding
Biology
Crystallography
X-Ray
chemistry [Schizosaccharomyces pombe Proteins]
Article
Protein Structure
Secondary
Adenosine Triphosphate
ddc:570
Hydrolase
Amino Acid Sequence
Binding site
Protein Structure
Quaternary
Peptide sequence
metabolism [Alanine]
Dcp1 protein
S pombe
Molecular Biology
Glutathione Transferase
Alanine
Binding Sites
Base Sequence
Small-angle X-ray scattering
Cell Biology
Protein Structure
Tertiary
Decapping complex
Biochemistry
Amino Acid Substitution
Structural Homology
Protein
metabolism [Schizosaccharomyces pombe Proteins]
Schizosaccharomyces pombe Proteins
genetics [Schizosaccharomyces pombe Proteins]
chemistry [Recombinant Fusion Proteins]
Protein Binding
Zdroj: Molecular cell 29, 337-349 (2008). doi:10.1016/j.molcel.2008.01.002
ISSN: 1097-2765
DOI: 10.1016/j.molcel.2008.01.002
Popis: Summary 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.
Databáze: OpenAIRE
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