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| [[Image:2qkl.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2qkl| PDB=2qkl | SCENE= }} | | {{STRUCTURE_2qkl| PDB=2qkl | SCENE= }} |
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| '''The crystal structure of fission yeast mRNA decapping enzyme Dcp1-Dcp2 complex'''
| | ===The crystal structure of fission yeast mRNA decapping enzyme Dcp1-Dcp2 complex=== |
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| ==Overview==
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| A critical step in mRNA degradation is the removal of the 5' cap structure, which is catalyzed by the Dcp1-Dcp2 complex. The crystal structure of an S. pombe Dcp1p-Dcp2n complex combined with small-angle X-ray scattering analysis (SAXS) reveals that Dcp2p exists in open and closed conformations, with the closed complex being, or closely resembling, the catalytically more active form. This suggests that a conformational change between these open and closed complexes might control decapping. A bipartite RNA-binding channel containing the catalytic site and Box B motif is identified with a bound ATP located in the catalytic pocket in the closed complex, suggesting possible interactions that facilitate substrate binding. Dcp1 stimulates the activity of Dcp2 by promoting and/or stabilizing the closed complex. Notably, the interface of Dcp1 and Dcp2 is not fully conserved, explaining why the Dcp1-Dcp2 interaction in higher eukaryotes requires an additional factor.
| | The line below this paragraph, {{ABSTRACT_PUBMED_18280239}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 18280239 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_18280239}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| [[Category: Protein-protein complex]] | | [[Category: Protein-protein complex]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 15:07:14 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 16 08:52:05 2008'' |