1irx
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, resolution 2.6Å | |||||||
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Ligands: | |||||||
Activity: | Lysine--tRNA ligase, with EC number 6.1.1.6 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of class I lysyl-tRNA synthetase
OverviewOverview
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.
About this StructureAbout this Structure
1IRX is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.
ReferenceReference
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
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OCA- Pages with broken file links
- Lysine--tRNA ligase
- Pyrococcus horikoshii
- Single protein
- 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
- Riken structural genomics/proteomics initiative
- Rossmann fold
- Rsgi
- Structural genomic
- Zinc-binding structure