2br2: Difference between revisions
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Revision as of 18:40, 5 November 2007
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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 CL as ligand. Structure known Active Site: AC1. 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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