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Crystal structure of class I lysyl-tRNA synthetaseCrystal structure of class I lysyl-tRNA synthetase
Structural highlights
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 PubMedLysyl-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. Functional convergence of two lysyl-tRNA synthetases with unrelated topologies.,Terada T, Nureki O, Ishitani R, Ambrogelly A, Ibba M, Soll D, Yokoyama S Nat Struct Biol. 2002 Apr;9(4):257-62. PMID:11887185[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Lysine--tRNA ligase
- Pyrococcus horikoshii
- Ambrogelly, A.
- Ibba, M.
- Ishitani, R.
- Nureki, O.
- RSGI, RIKEN Structural Genomics/Proteomics Initiative.
- Soll, D.
- Terada, T.
- Yokoyama, S.
- Alpha-helix cage
- Beta sandwitch
- Ligase
- Riken structural genomics/proteomics initiative
- Rossmann fold
- Rsgi
- Structural genomic
- Zinc-binding structure