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.

• PMID: 7664121
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Reference Type

Comparative Study | Journal Article | Research Support, Non-U.S. Gov't

Authors

Mosyak L, Reshetnikova L, Goldgur Y, Delarue M, Safro MG

Primary Lit For

Phenylalanyl-tRNA synthetase complex

Additional Lit For

Review For