2QKL

The crystal structure of fission yeast mRNA decapping enzyme Dcp1-Dcp2 complex

Summary for 2QKL

• Entry DOI: 10.2210/pdb2qkl/pdb
• Descriptor: SPBC3B9.21 protein, SPAC19A8.12 protein, LEAD (II) ION, ... (4 entities in total)
• Functional Keywords: protein-protein complex, hydrolase
• Biological source: Schizosaccharomyces pombe (fission yeast); More
• Cellular location: Cytoplasm: Q9P805; Cytoplasm, P-body: O13828
• Total number of polymer chains: 2
• Total formula weight: 26512.12

Authors

She, M.,Chen, N.,Song, H. (deposition date: 2007-07-11, release date: 2008-03-25, Last modification date: 2024-02-21)

Primary citation

She, M.,Decker, C.J.,Svergun, D.I.,Round, A.,Chen, N.,Muhlrad, D.,Parker, R.,Song, H.
Structural basis of dcp2 recognition and activation by dcp1.
Mol.Cell, 29:337-349, 2008

PubMed 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.

PubMed: 18280239
DOI: 10.1016/j.molcel.2008.01.002

Experimental method

X-RAY DIFFRACTION (2.33 Å)