| Literature DB >> 11887185 |
Takaho Terada1, Osamu Nureki, Ryuichiro Ishitani, Alexandre Ambrogelly, Michael Ibba, Dieter Söll, Shigeyuki Yokoyama.
Abstract
Lysyl-tRNA can be synthesized by both a class I (LysRS-I) and a class II (LysRS-II) lysyl-tRNA synthetase. The crystal structure of LysRS-I from Pyrococcus horikoshii at 2.6 A resolution reveals extensive similarity with glutamyl-tRNA synthetase (GluRS). A comparison of the structures of LysRS-I and LysRS-II in complex with lysine shows that both enzymes use similar strategies for substrate recognition within unrelated active site topologies. A docking model based upon the GluRS-tRNA complex suggests how LysRS-I and LysRS-II can recognize the same molecular determinants in tRNALys, as shown by biochemical results, while approaching the acceptor helix of the tRNA from opposite sides.Entities:
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Year: 2002 PMID： 11887185 DOI： 10.1038/nsb777
Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368