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http://dx.doi.org/10.5012/bkcs.2007.28.2.207

Three Common Subunits in Editing Domains of Class Ia tRNA Synthetases  

Lee, Keun-Woo (Department of Biochemistry, Division of Applied Life Science, Environmental Biotechnology National Core Research Center (EB-NCRC), Plant Molecular Biology and Biotechnology Research Center (PMBBRC), Gyeongsang National University)
Kwon, Yong-Jung (Department of Chemical Engineering, Kangwon National University)
Briggs, James M. (Department of Biology and Biochemistry, University of Houston)
Publication Information
Bulletin of the Korean Chemical Society / v.28, no.2, 2007 , pp. 207-210 More about this Journal
Abstract
To identify structural or functional common subunit(s) in the CP1 (editing) domains of class Ia tRNA synthetases, five available structures were compared and analyzed. Through the sequence alignments and structural overlapping of the CP1 domains, three conserved regions were identified near the amino acid binding site in the editing domain. Structural overlapping of the three subunits clearly showed the existence of three common structural subunits in all of the five editing RS structures. Based on the established experimental results and our modeling results, it is proposed that subunits 1 and 3 accommodate the incoming amino acid binding, while subunit 2 contributes to the interactions with the adenosine ring of the A76 to stabilize the overall tRNA binding. Since these subunits are critical for the editing reaction, we expect that these key structures should be conserved through the most class Ia editing RSs.
Keywords
Aminoacyl-tRNA synthetase (aaRS); Editing domain; Aminoacylation; CP1 domain;
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