3G10
Structure of S. pombe Pop2p - Mg2+ and Mn2+ bound form
3G10 の概要
| エントリーDOI | 10.2210/pdb3g10/pdb |
| 関連するPDBエントリー | 3G0Z |
| 分子名称 | CCR4-Not complex subunit Caf1, MAGNESIUM ION, MANGANESE (II) ION, ... (4 entities in total) |
| 機能のキーワード | mrna turnover, deadenylation, ccr4-not, pop2p, caf1p, dedd exonuclease, hydrolase, gene regulation |
| 由来する生物種 | Schizosaccharomyces pombe (Fission yeast) |
| 細胞内の位置 | Cytoplasm : O74856 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 37396.17 |
| 構造登録者 | Andersen, K.R.,Jonstrup, A.T.,Van, L.B.,Brodersen, D.E. (登録日: 2009-01-29, 公開日: 2009-03-31, 最終更新日: 2023-11-01) |
| 主引用文献 | Andersen, K.R.,Jonstrup, A.T.,Van, L.B.,Brodersen, D.E. The activity and selectivity of fission yeast Pop2p are affected by a high affinity for Zn2+ and Mn2+ in the active site Rna, 15:850-861, 2009 Cited by PubMed Abstract: In eukaryotic organisms, initiation of mRNA turnover is controlled by progressive shortening of the poly-A tail, a process involving the mega-Dalton Ccr4-Not complex and its two associated 3'-5' exonucleases, Ccr4p and Pop2p (Caf1p). RNA degradation by the 3'-5' DEDDh exonuclease, Pop2p, is governed by the classical two metal ion mechanism traditionally assumed to be dependent on Mg(2+) ions bound in the active site. Here, we show biochemically and structurally that fission yeast (Schizosaccharomyces pombe) Pop2p prefers Mn(2+) and Zn(2+) over Mg(2+) at the concentrations of the ions found inside cells and that the identity of the ions in the active site affects the activity of the enzyme. Ion replacement experiments further suggest that mRNA deadenylation could be subtly regulated by local Zn(2+) levels in the cell. Finally, we use site-directed mutagenesis to propose a mechanistic model for the basis of the preference for poly-A sequences exhibited by the Pop2p-type deadenylases as well as their distributive enzymatic behavior. PubMed: 19307292DOI: 10.1261/rna.1489409 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.597 Å) |
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