Download MendeleyStructure of phenylalanyl-tRNA synthetase from Thermus thermophilus.
Mosyak, L., Reshetnikova, L., Goldgur, Y., Delarue, M., Safro, M.G.(1995) Nat Struct Biol 2: 537-547
- PubMed: 7664121
- DOI: https://doi.org/10.1038/nsb0795-537
- Primary Citation of Related Structures:
1PYS - PubMed Abstract:
The crystal structure of phenylalanyl-tRNA synthetase from Thermus thermophilus, solved at 2.9 A resolution, displays (alpha beta)2 subunit organization. Unexpectedly, both the catalytic alpha- and the non-catalytic beta-subunits comprise the characteristic fold of the class II active-site domains. The alpha beta heterodimer contains most of the building blocks so far identified in the class II synthetases. The presence of an RNA-binding domain, similar to that of the U1A spliceosomal protein, in the beta-subunit is indicative of structural relationships among different families of RNA-binding proteins. The structure suggests a plausible catalytic mechanism which explains why the primary site of tRNA aminoacylation is different from that of the other class II enzymes.
Organizational Affiliation:
Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
