2wnr

The structure of Methanothermobacter thermautotrophicus exosome core assembly

spinqualitylabelsall models 2wnr, resolution 2.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wnr is a 6 chain structure with sequence from "methanobacterium_thermoautotrophicus"_(sic)_zeikus_and_wolfe_1972 "methanobacterium thermoautotrophicus" (sic) zeikus and wolfe 1972. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RRP42_METTH] Non-catalytic component of the exosome, which is a complex involved in RNA degradation. Contributes to the structuring of the Rrp41 active site.[HAMAP-Rule:MF_00622] [RRP41_METTH] Catalytic component of the exosome, which is a complex involved in RNA degradation. Has 3'->5' exoribonuclease activity. Can also synthesize heteropolymeric RNA-tails.[HAMAP-Rule:MF_00591] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The core of the exosome, a versatile multisubunit RNA-processing enzyme found in archaea and eukaryotes, includes a ring of six RNase PH subunits. This basic architecture is homologous to those of the bacterial and archaeal RNase PHs and the bacterial polynucleotide phosphorylase (PNPase). While all six RNase PH monomers are catalytically active in the homohexameric RNase PH, only half of them are functional in the bacterial PNPase and in the archaeal exosome core and none are functional in the yeast and human exosome cores. Here, the crystal structure of the RNase PH ring from the exosome of the anaerobic methanogenic archaeon Methanothermobacter thermautotrophicus is described at 2.65 A resolution. Free phosphate anions were found for the first time in the active sites of the RNase PH subunits of an exosome structure and provide structural snapshots of a critical intermediate in the phosphorolytic degradation of RNA by the exosome. Furthermore, the present structure highlights the plasticity of the surfaces delineating the polar regions of the RNase PH ring of the exosome, a feature that can facilitate both interaction with the many cofactors involved in exosome function and the processive activity of this enzyme. Structure of the Methanothermobacter thermautotrophicus exosome RNase PH ring.,Ng CL, Waterman DG, Antson AA, Ortiz-Lombardia M Acta Crystallogr D Biol Crystallogr. 2010 May;66(Pt 5):522-8. Epub 2010, Apr 21. PMID:20445227 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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