1IRX

Crystal structure of class I lysyl-tRNA synthetase

Summary for 1IRX

• Entry DOI: 10.2210/pdb1irx/pdb
• Descriptor: lysyl-tRNA synthetase, ZINC ION (3 entities in total)
• Functional Keywords: beta sandwitch, zinc-binding structure, rossmann fold, alpha-helix cage, riken structural genomics/proteomics initiative, rsgi, structural genomics, ligase
• Biological source: Pyrococcus horikoshii
• Cellular location: Cytoplasm: O57963
• Total number of polymer chains: 2
• Total formula weight: 123574.44

Authors

Nureki, O.,Terada, T.,Ishitani, R.,Ambrogelly, A.,Ibba, M.,Soll, D.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2001-10-25, release date: 2002-04-17, Last modification date: 2023-12-27)

Primary citation

Terada, T.,Nureki, O.,Ishitani, R.,Ambrogelly, A.,Ibba, M.,Soll, D.,Yokoyama, S.
Functional convergence of two lysyl-tRNA synthetases with unrelated topologies.
Nat.Struct.Biol., 9:257-262, 2002

PubMed 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.

PubMed: 11887185
DOI: 10.1038/nsb777

Experimental method

X-RAY DIFFRACTION (2.6 Å)