Summary information and primary citation

PDB-id
2fk6; SNAP-derived features in text and JSON formats; DNAproDB
Class
hydrolase-RNA
Method
X-ray (2.9 Å)
Summary
Crystal structure of rnase z-trna(thr) complex
Reference
Li de la Sierra-Gallay I, Mathy N, Pellegrini O, Condon C (2006): "Structure of the ubiquitous 3' processing enzyme RNase Z bound to transfer RNA." Nat.Struct.Mol.Biol., 13, 376-377. doi: 10.1038/nsmb1066.
Abstract
The highly conserved ribonuclease RNase Z catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Here we present the structure of the complex between Bacillus subtilis RNase Z and tRNA(Thr), the first structure of a ribonucleolytic processing enzyme bound to tRNA. Binding of tRNA to RNase Z causes conformational changes in both partners to promote reorganization of the catalytic site and tRNA cleavage.

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