The 1.4-Å crystal structure of the S. pombe Pop2p deadenylase subunit unveils the configuration of an active enzyme

@inproceedings{Jonstrup2007The1C,
  title={The 1.4-{\AA} crystal structure of the S. pombe Pop2p deadenylase subunit unveils the configuration of an active enzyme},
  author={Anette Thyssen Jonstrup and Kasper R\ojkj{\ae}r Andersen and Lan Bich Van and Ditlev Egeskov Brodersen},
  booktitle={Nucleic acids research},
  year={2007}
}
Deadenylation is the first and probably also rate-limiting step of controlled mRNA decay in eukaryotes and therefore central for the overall rate of gene expression. In yeast, the process is maintained by the mega-Dalton Ccr4-Not complex, of which both the Ccr4p and Pop2p subunits are 3'-5' exonucleases potentially responsible for the deadenylation reaction. Here, we present the crystal structure of the Pop2p subunit from Schizosaccharomyces pombe determined to 1.4 A resolution and show that… CONTINUE READING

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