2qkl: Difference between revisions

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[[Image:2qkl.~~jpg~~|left|200px]]

[[Image:2qkl.png|left|200px]]

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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===

~~==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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==About this Structure==

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[[Category: Hydrolase]]

[[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''

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-[[Image:2qkl.jpg|left|200px]]
+{{Seed}}
+[[Image:2qkl.png|left|200px]]
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 {{STRUCTURE_2qkl|  PDB=2qkl  |  SCENE=  }}
-'''The crystal structure of fission yeast mRNA decapping enzyme Dcp1-Dcp2 complex'''
+===The crystal structure of fission yeast mRNA decapping enzyme Dcp1-Dcp2 complex===
-==Overview==
+<!--
-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.
+-->
+{{ABSTRACT_PUBMED_18280239}}
 ==About this Structure==
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 [[Category: Hydrolase]]
 [[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''