2c38: Difference between revisions

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==Overview==

The exosome is a macromolecular complex that plays fundamental roles in, the biogenesis and turnover of a large number of RNA species. Here we, report the crystal structures of the Rrp41-Rrp42 core complex of the S., solfataricus exosome bound to short single-stranded RNAs and to ADP. The, RNA binding cleft recognizes four nucleotides in a sequence-unspecific, manner, mainly by electrostatic interactions with the phosphate groups., Interactions at the 2' hydroxyls of the sugars provide specificity for RNA, over DNA. The structures show both the bound substrate and the cleaved, product of the reaction, suggesting a catalytic mechanism for the 3'-5', phosphorolytic activity of the exosome.

The exosome is a macromolecular complex that plays fundamental roles in the biogenesis and turnover of a large number of RNA species. Here we report the crystal structures of the Rrp41-Rrp42 core complex of the S. solfataricus exosome bound to short single-stranded RNAs and to ADP. The RNA binding cleft recognizes four nucleotides in a sequence-unspecific manner, mainly by electrostatic interactions with the phosphate groups. Interactions at the 2' hydroxyls of the sugars provide specificity for RNA over DNA. The structures show both the bound substrate and the cleaved product of the reaction, suggesting a catalytic mechanism for the 3'-5' phosphorolytic activity of the exosome.

==About this Structure==

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[[Category: rrp42]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The exosome is a macromolecular complex that plays fundamental roles in, the biogenesis and turnover of a large number of RNA species. Here we, report the crystal structures of the Rrp41-Rrp42 core complex of the S., solfataricus exosome bound to short single-stranded RNAs and to ADP. The, RNA binding cleft recognizes four nucleotides in a sequence-unspecific, manner, mainly by electrostatic interactions with the phosphate groups., Interactions at the 2' hydroxyls of the sugars provide specificity for RNA, over DNA. The structures show both the bound substrate and the cleaved, product of the reaction, suggesting a catalytic mechanism for the 3'-5', phosphorolytic activity of the exosome.
+The exosome is a macromolecular complex that plays fundamental roles in the biogenesis and turnover of a large number of RNA species. Here we report the crystal structures of the Rrp41-Rrp42 core complex of the S. solfataricus exosome bound to short single-stranded RNAs and to ADP. The RNA binding cleft recognizes four nucleotides in a sequence-unspecific manner, mainly by electrostatic interactions with the phosphate groups. Interactions at the 2' hydroxyls of the sugars provide specificity for RNA over DNA. The structures show both the bound substrate and the cleaved product of the reaction, suggesting a catalytic mechanism for the 3'-5' phosphorolytic activity of the exosome.
 ==About this Structure==
@@ Line 29: / Line 29: @@
 [[Category: rrp42]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:30:52 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:44:22 2008''