2A6T: Crystal Structure of S.pombe mRNA Decapping Enzyme Dcp2p

Citation:
Abstract
Decapping is a key step in both general and nonsense-mediated 5' --> 3' mRNA-decay pathways. Removal of the cap structure is catalyzed by the Dcp1-Dcp2 complex. The crystal structure of a C-terminally truncated Schizosaccharomyces pombe Dcp2p reveals two distinct domains: an all-helical N-terminal domain and a C-terminal domain that is a classic Nudix fold. The C-terminal domain of both Saccharomyces cerevisiae and S. pombe Dcp2p proteins is sufficient for decapping activity, although the N-terminal domain can affect the efficiency of Dcp2p function. The binding of Dcp2p to Dcp1p is mediated by a conserved surface on its N-terminal domain, and the N-terminal domain is required for Dcp1p to stimulate Dcp2p activity. The flexible nature of the N-terminal domain relative to the C-terminal domain suggests that Dcp1p binding to Dcp2p may regulate Dcp2p activity through conformational changes of the two domains.
PDB ID: 2A6TDownload
MMDB ID: 36664
PDB Deposition Date: 2005/7/4
Updated in MMDB: 2012/10 
Experimental Method:
x-ray diffraction
Resolution: 2.5  Å
Source Organism:
Similar Structures:
Biological Unit for 2A6T: monomeric; determined by author
Molecular Components in 2A6T
Label Count Molecule
Protein (1 molecule)
1
Spac19a8.12
(Gene: dcp2)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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