2A6T

Crystal structure of S.pombe mRNA decapping enzyme Dcp2p

2A6T の概要

• エントリーDOI: 10.2210/pdb2a6t/pdb
• 分子名称: SPAC19A8.12 (2 entities in total)
• 機能のキーワード: alpha/beta/alpha, rna binding protein, hydrolase
• 由来する生物種: Schizosaccharomyces pombe (fission yeast)
• 細胞内の位置: Cytoplasm, P-body: O13828
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 62716.17

構造登録者

She, M.,Chen, N.,Song, H. (登録日: 2005-07-04, 公開日: 2005-12-20, 最終更新日: 2024-03-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.5 Å)