2ALY

Crystal Structure of T.Thermophilus Phenylalanyl-tRNA synthetase complexed with 5'-O-[N-(L-tyrosyl)sulphamoyl]adenosine

Summary for 2ALY

• Entry DOI: 10.2210/pdb2aly/pdb
• Related: 1b70 1b7y 1eiy 1jjc 1pys 2akw
• Descriptor: Phenylalanyl-tRNA synthetase alpha chain, Phenylalanyl-tRNA synthetase beta chain, MANGANESE (II) ION, ... (6 entities in total)
• Functional Keywords: protein-ligand complex, ligase
• Biological source: Thermus thermophilus; More
• Cellular location: Cytoplasm: P27001 P27002
• Total number of polymer chains: 2
• Total formula weight: 117336.53

Authors

Kotik-Kogan, O.M.,Moor, N.A.,Tworowski, D.E.,Safro, M.G. (deposition date: 2005-08-04, release date: 2005-12-27, Last modification date: 2024-02-14)

Primary citation

Kotik-Kogan, O.M.,Moor, N.A.,Tworowski, D.E.,Safro, M.G.
Structural Basis for Discrimination of L-Phenylalanine from L-Tyrosine by Phenylalanyl-tRNA Synthetase
Structure, 13:1799-1807, 2005

PubMed Abstract: Aminoacyl-tRNA synthetases (aaRSs) exert control over the faithful transfer of amino acids onto cognate tRNAs. Since chemical structures of various amino acids closely resemble each other, it is difficult to discriminate between them. Editing activity has been evolved by certain aaRSs to resolve the problem. In this study, we determined the crystal structures of complexes of T. thermophilus phenylalanyl-tRNA synthetase (PheRS) with L-tyrosine, p-chloro-phenylalanine, and a nonhydrolyzable tyrosyl-adenylate analog. The structures demonstrate plasticity of the synthetic site capable of binding substrates larger than phenylalanine and provide a structural basis for the proofreading mechanism. The editing site is localized at the B3/B4 interface, 35 A from the synthetic site. Glubeta334 plays a crucial role in the specific recognition of the Tyr moiety in the editing site. The tyrosyl-adenylate analog binds exclusively in the synthetic site. Both structural data and tyrosine-dependent ATP hydrolysis enhanced by tRNA(Phe) provide evidence for a preferential posttransfer editing pathway in the phenylalanine-specific system.

PubMed: 16338408
DOI: 10.1016/j.str.2005.08.013

Experimental method

X-RAY DIFFRACTION (2.6 Å)