2c37

RNASE PH CORE OF THE ARCHAEAL EXOSOME IN COMPLEX WITH U8 RNA

spinqualitylabelsall models 2c37, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2c37 is a 24 chain structure with sequence from Atcc 35091. The February 2007 RCSB PDB Molecule of the Month feature on Exosomes by David S. Goodsell is 10.2210/rcsb_pdb/mom_2007_2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, NA, RP5, U5P Related: 2br2, 2c38, 2c39 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [ECX2_SULSO] Probably involved in the 3'->5' degradation of a variety of RNA species (Potential). [ECX1_SULSO] Probably involved in the 3'->5' degradation of a variety of RNA species (Potential). 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 exosome is a macromolecular complex that plays fundamental roles in the biogenesis and turnover of a large number of RNA species. Here we report the crystal structures of the Rrp41-Rrp42 core complex of the S. solfataricus exosome bound to short single-stranded RNAs and to ADP. The RNA binding cleft recognizes four nucleotides in a sequence-unspecific manner, mainly by electrostatic interactions with the phosphate groups. Interactions at the 2' hydroxyls of the sugars provide specificity for RNA over DNA. The structures show both the bound substrate and the cleaved product of the reaction, suggesting a catalytic mechanism for the 3'-5' phosphorolytic activity of the exosome. Structural basis of 3' end RNA recognition and exoribonucleolytic cleavage by an exosome RNase PH core.,Lorentzen E, Conti E Mol Cell. 2005 Nov 11;20(3):473-81. PMID:16285928 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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