Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Crystal structure and functional analysis of Dcp2p from Schizosaccharomyces pombe.

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 ID: 16341225


  • She M
  • Decker CJ
  • Chen N
  • Tumati S
  • Parker R
  • Song H


Nature structural & molecular biology

Publication Data

January 5, 2006

Associated Grants

  • Agency: NIGMS NIH HHS, Id: R37 GM045443

Mesh Terms

  • Catalysis
  • Crystallography, X-Ray
  • Models, Molecular
  • Protein Binding
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Pyrophosphatases
  • Schizosaccharomyces
  • Schizosaccharomyces pombe Proteins
  • Structural Homology, Protein