2a6t
From Proteopedia
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| , resolution 2.50Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of S.pombe mRNA decapping enzyme Dcp2p
Overview
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.
About this Structure
2A6T is a Single protein structure of sequence from Schizosaccharomyces pombe. Full crystallographic information is available from OCA.
Reference
Crystal structure and functional analysis of Dcp2p from Schizosaccharomyces pombe., She M, Decker CJ, Chen N, Tumati S, Parker R, Song H, Nat Struct Mol Biol. 2006 Jan;13(1):63-70. Epub 2005 Dec 11. PMID:16341225
Page seeded by OCA on Thu Mar 20 15:46:03 2008
