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Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus

Nature Structural Biology volume 2, pages 537–547 (1995)Cite this article

Abstract

The crystal structure of phenylalanyl-tRNA synthetase from Thermus thermophilus, solved at 2.9 Å resolution, displays (αβ)2 subunit organization. Unexpectedly, both the catalytic α- and the non-catalytic β-subunits comprise the characteristic fold of the class II active-site domains. The αβ heterodimer contains most of the building blocks so far identified in the class II synthetases. The presence of an RNA-binding domain, similiar to that of the U1A spliceosomal protein, in the β-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 tRIMA aminoacylation is different from that of the other class II enzymes.

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Authors and Affiliations

  1. Department of Structural Biology, Weizmann Institute of Science, Rehovot, 76100, Israel

    Lidia Mosyak, Yehuda Goldgur & Mark G. Safro

  2. Institute of Molecular Biology, Moscow, 117984, Russia

    Ludmila Reshetnikova

  3. Unite d'lmmunologie Structural, Institut Pasteur, Paris, 75015, France

    Marc Delarue

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  1. Lidia Mosyak
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  4. Marc Delarue
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  5. Mark G. Safro
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Mosyak, L., Reshetnikova, L., Goldgur, Y. et al. Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus. Nat Struct Mol Biol 2, 537–547 (1995). https://doi.org/10.1038/nsb0795-537

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