2ba0: Difference between revisions

Revision as of 16:22, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ba0.png

Template:STRUCTURE 2ba0

Archaeal exosome coreArchaeal exosome core

Template:ABSTRACT PUBMED 16285927

About this StructureAbout this Structure

2BA0 is a Protein complex structure of sequences from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.

ReferenceReference

Structural framework for the mechanism of archaeal exosomes in RNA processing., Buttner K, Wenig K, Hopfner KP, Mol Cell. 2005 Nov 11;20(3):461-71. PMID:16285927

Page seeded by OCA on Sun Jul 27 16:22:23 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Archaeal exosome core'''
+===Archaeal exosome core===
-==Overview==
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-Exosomes emerge as central 3'--&gt;5' RNA processing and degradation machineries in eukaryotes and archaea. We determined crystal structures of two 230 kDa nine subunit archaeal exosome isoforms. Both exosome isoforms contain a hexameric ring of RNase phosphorolytic (PH) domain subunits with a central chamber. Tungstate soaks identified three phosphorolytic active sites in this processing chamber. A trimer of Csl4 or Rrp4 subunits forms a multidomain macromolecular interaction surface on the RNase-PH domain ring with central S1 domains and peripheral KH and zinc-ribbon domains. Structural and mutational analyses suggest that the S1 domains and a subsequent neck in the RNase-PH domain ring form an RNA entry pore to the processing chamber that only allows access of unstructured RNA. This structural framework can mechanistically unify observed features of exosomes, including processive degradation of unstructured RNA, the requirement for regulatory factors to degrade structured RNA, and left-over tails in rRNA trimming.
+The line below this paragraph, {{ABSTRACT_PUBMED_16285927}}, adds the Publication Abstract to the page
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 [[Category: Rnase ph]]
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