1EIY

THE CRYSTAL STRUCTURE OF PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH COGNATE TRNAPHE

Summary for 1EIY

• Entry DOI: 10.2210/pdb1eiy/pdb
• Related: 1PYS
• Descriptor: TRNA(PHE), PHENYLALANYL-TRNA SYNTHETASE (3 entities in total)
• Functional Keywords: aminoacyl-trna synthetase, trna recognition, ligase-rna complex, ligase/rna
• Biological source: Thermus thermophilus; More
• Cellular location: Cytoplasm: P27001 Q5SGX2 Q5SGX1
• Total number of polymer chains: 3
• Total formula weight: 150514.41

Authors

Goldgur, Y.,Mosyak, L.,Reshetnikova, L.,Ankilova, V.,Safro, M. (deposition date: 2000-02-29, release date: 2000-03-06, Last modification date: 2024-02-07)

Primary citation

Goldgur, Y.,Mosyak, L.,Reshetnikova, L.,Ankilova, V.,Lavrik, O.,Khodyreva, S.,Safro, M.
The crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus complexed with cognate tRNAPhe.
Structure, 5:59-68, 1997

PubMed Abstract: In the translation of the genetic code each aminoacyl-tRNA synthetase (aaRS) must recognize its own (cognate) tRNA and attach the corresponding amino acid to the acceptor end of tRNA, discriminating all the others. The(alphabeta)2 phenylalanyl-tRNA synthetase (PheRS) is one of the most complex enzymes in the aaRS family and is characterized by anomalous charging properties. Structurally, the enzyme belongs to class II aaRSs, as its catalytic domain is built around an antiparallel beta sheet, but functionally it resembles class I as it aminoacylates the 2'OH of the terminal ribose of tRNA (class II aaRSs aminoacylate the 3'OH). With the availability of the three-dimensional structure of the complex between multisubunit PheRS and tRNAPhe, a fuller picture of the specific tRNA-aaRS interactions is beginning to emerge.

PubMed: 9016717
DOI: 10.1016/S0969-2126(97)00166-4

Experimental method

X-RAY DIFFRACTION (3.3 Å)