• Register
X
Forgot Password

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

X

Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.

No
Yes

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

Authors

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

Journal

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