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Nat Struct Biol. 1995 Jul;2(7):537-47.

Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus.

Author information

1
Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.

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.

PMID:
7664121
[Indexed for MEDLINE]

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