Table of Contents
Journal of Amino Acids
Volume 2010, Article ID 983503, 7 pages
Review Article

Structural Aspects of Phenylalanylation and Quality Control in Three Major Forms of Phenylalanyl-tRNA Synthetase

1Department of Structural Biology, Weizmann Institute of Science, P.O. Box 26, 76100 Rehovot, Israel
2Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of Russian Academy of Sciences (RAS), Novosibirsk 630090, Russia

Received 26 March 2010; Accepted 28 May 2010

Academic Editor: Hieronim Jakubowski

Copyright © 2010 Liron Klipcan et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Aminoacyl-tRNA synthetases (aaRSs) are a canonical set of enzymes that specifically attach corresponding amino acids to their cognate transfer RNAs in the cytoplasm, mitochondria, and nucleus. The aaRSs display great differences in primary sequence, subunit size, and quaternary structure. Existence of three types of phenylalanyl-tRNA synthetase (PheRS)—bacterial , eukaryotic/archaeal cytosolic , and mitochondrial —is a prominent example of structural diversity within the aaRSs family. Although archaeal/eukaryotic and bacterial PheRSs share common topology of the core domains and the B3/B4 interface, where editing activity of heterotetrameric PheRSs is localized, the detailed investigation of the three-dimensional structures from three kingdoms revealed significant variations in the local design of their synthetic and editing sites. Moreover, as might be expected from structural data eubacterial, Thermus thermophilus and human cytoplasmic PheRSs acquire different patterns of tRN anticodon recognition.