2po2 | pdb_00002po2

Crystal structure of the P. abyssi exosome RNase PH ring complexed with CDP

spinqualitylabelsall models 2po2, resolution 2.41Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2po2 is a 2 chain structure with sequence from "pyrococcus_abyssi"_erauso_et_al._1993 "pyrococcus abyssi" erauso et al. 1993. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CDP, MPD Related: 2pnz, 2po0, 2po1 Gene: Rrp41 ("Pyrococcus abyssi" Erauso et al. 1993), Rrp42 ("Pyrococcus abyssi" Erauso et al. 1993) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RRP41_PYRAB] Catalytic component of the exosome, which is a complex involved in RNA degradation. Has 3'->5' exoribonuclease activity. Can also synthesize heteropolymeric RNA-tails (Probable). [RRP42_PYRAB] 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] 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 Initially identified in yeast, the exosome has emerged as a central component of the RNA maturation and degradation machinery both in Archaea and eukaryotes. Here we describe a series of high-resolution structures of the RNase PH ring from the Pyrococcus abyssi exosome, one of them containing three 10-mer RNA strands within the exosome catalytic chamber, and report additional nucleotide interactions involving positions N5 and N7. Residues from all three Rrp41-Rrp42 heterodimers interact with a single RNA molecule, providing evidence for the functional relevance of exosome ring-like assembly in RNA processivity. Furthermore, an ADP-bound structure showed a rearrangement of nucleotide interactions at site N1, suggesting a rationale for the elimination of nucleoside diphosphate after catalysis. In combination with RNA degradation assays performed with mutants of key amino acid residues, the structural data presented here provide support for a model of exosome-mediated RNA degradation that integrates the events involving catalytic cleavage, product elimination, and RNA translocation. Finally, comparisons between the archaeal and human exosome structures provide a possible explanation for the eukaryotic exosome inability to catalyze phosphate-dependent RNA degradation. Insights into the mechanism of progressive RNA degradation by the archaeal exosome.,Navarro MV, Oliveira CC, Zanchin NI, Guimaraes BG J Biol Chem. 2008 May 16;283(20):14120-31. Epub 2008 Mar 19. PMID:18353775 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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