2br2: Difference between revisions

Revision as of 17:40, 21 February 2008

RNASE PH CORE OF THE ARCHAEAL EXOSOME

OverviewOverview

The exosome is a 3' --> 5' exoribonuclease complex involved in RNA processing. We report the crystal structure of the RNase PH core complex of the Sulfolobus solfataricus exosome determined at a resolution of 2.8 A. The structure reveals a hexameric ring-like arrangement of three Rrp41-Rrp42 heterodimers, where both subunits adopt the RNase PH fold common to phosphorolytic exoribonucleases. Structure-guided mutagenesis reveals that the activity of the complex resides within the active sites of the Rrp41 subunits, all three of which face the same side of the hexameric structure. The Rrp42 subunit is inactive but contributes to the structuring of the Rrp41 active site. The high sequence similarity of this archaeal exosome to eukaryotic exosomes and its high structural similarity to the bacterial mRNA-degrading PNPase support a common basis for RNA-degrading machineries in all three domains of life.

About this StructureAbout this Structure

2BR2 is a Protein complex structure of sequences from Sulfolobus solfataricus with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

The archaeal exosome core is a hexameric ring structure with three catalytic subunits., Lorentzen E, Walter P, Fribourg S, Evguenieva-Hackenberg E, Klug G, Conti E, Nat Struct Mol Biol. 2005 Jul;12(7):575-81. Epub 2005 Jun 12. PMID:15951817

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 ==Overview==
-The exosome is a 3' --&gt; 5' exoribonuclease complex involved in RNA, processing. We report the crystal structure of the RNase PH core complex, of the Sulfolobus solfataricus exosome determined at a resolution of 2.8, A. The structure reveals a hexameric ring-like arrangement of three, Rrp41-Rrp42 heterodimers, where both subunits adopt the RNase PH fold, common to phosphorolytic exoribonucleases. Structure-guided mutagenesis, reveals that the activity of the complex resides within the active sites, of the Rrp41 subunits, all three of which face the same side of the, hexameric structure. The Rrp42 subunit is inactive but contributes to the, structuring of the Rrp41 active site. The high sequence similarity of this, archaeal exosome to eukaryotic exosomes and its high structural similarity, to the bacterial mRNA-degrading PNPase support a common basis for, RNA-degrading machineries in all three domains of life.
+The exosome is a 3' --&gt; 5' exoribonuclease complex involved in RNA processing. We report the crystal structure of the RNase PH core complex of the Sulfolobus solfataricus exosome determined at a resolution of 2.8 A. The structure reveals a hexameric ring-like arrangement of three Rrp41-Rrp42 heterodimers, where both subunits adopt the RNase PH fold common to phosphorolytic exoribonucleases. Structure-guided mutagenesis reveals that the activity of the complex resides within the active sites of the Rrp41 subunits, all three of which face the same side of the hexameric structure. The Rrp42 subunit is inactive but contributes to the structuring of the Rrp41 active site. The high sequence similarity of this archaeal exosome to eukaryotic exosomes and its high structural similarity to the bacterial mRNA-degrading PNPase support a common basis for RNA-degrading machineries in all three domains of life.
 ==About this Structure==
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 [[Category: rnase ph]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:26:54 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:40:43 2008''