2A6T

Crystal structure of S.pombe mRNA decapping enzyme Dcp2p

Summary for 2A6T

• Entry DOI: 10.2210/pdb2a6t/pdb
• Descriptor: SPAC19A8.12 (2 entities in total)
• Functional Keywords: alpha/beta/alpha, rna binding protein, hydrolase
• Biological source: Schizosaccharomyces pombe (fission yeast)
• Cellular location: Cytoplasm, P-body: O13828
• Total number of polymer chains: 2
• Total formula weight: 62716.17

Authors

She, M.,Chen, N.,Song, H. (deposition date: 2005-07-04, release date: 2005-12-20, Last modification date: 2024-03-13)

Primary citation

She, M.,Decker, C.J.,Chen, N.,Tumati, S.,Parker, R.,Song, H.
Crystal structure and functional analysis of Dcp2p from Schizosaccharomyces pombe
Nat.Struct.Mol.Biol., 13:63-70, 2006

PubMed 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.

PubMed: 16341225
DOI: 10.1038/nsmb1033

Experimental method

X-RAY DIFFRACTION (2.5 Å)