3g8q | pdb_00003g8q

A cytidine deaminase edits C-to-U in transfer RNAs in archaea

spinqualitylabelsall models 3g8q, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3g8q is a 4 chain structure with sequence from Methanopyrus kandleri. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NA, ZN Gene: MK0935 (Methanopyrus kandleri) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed All canonical transfer RNAs (tRNAs) have a uridine at position 8, involved in maintaining tRNA tertiary structure. However, the hyperthermophilic archaeon Methanopyrus kandleri harbors 30 (out of 34) tRNA genes with cytidine at position 8. Here, we demonstrate C-to-U editing at this location in the tRNA's tertiary core, and present the crystal structure of a tRNA-specific cytidine deaminase, CDAT8, which has the cytidine deaminase domain linked to a tRNA-binding THUMP domain. CDAT8 is specific for C deamination at position 8, requires only the acceptor stem hairpin for activity, and belongs to a unique family within the "cytidine deaminase-like" superfamily. The presence of this C-to-U editing enzyme guarantees the proper folding and functionality of all M. kandleri tRNAs. A cytidine deaminase edits C to U in transfer RNAs in Archaea.,Randau L, Stanley BJ, Kohlway A, Mechta S, Xiong Y, Soll D Science. 2009 May 1;324(5927):657-9. PMID:19407206 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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