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Structural Basis of the Initial Binding of tRNAIle Lysidine Synthetase TilS with ATP and L-Lysine

By Mitsuo Kuratani, Yuka Yoshikawa, Yoshitaka Bessho, Kyoko Higashijima, Takeshi Ishii, Rie Shibata, Seizo Takahashi, Katsuhide Yutani and Shigeyuki Yokoyama

Abstract

SummaryIn the bacterial genetic-code system, the codon AUA is decoded as isoleucine by tRNAIle2 with the lysidine residue at the wobble position. Lysidine is derived from cytidine, with ATP and L-lysine, by tRNAIle lysidine synthetase (TilS), which is an N-type ATP pyrophosphatase. In this study, we determined the crystal structure of Aquifex aeolicus TilS, complexed with ATP, Mg2+, and L-lysine, at 2.5 Å resolution. The presence of the TilS-specific subdomain causes the active site to have two separate gateways, a large hole and a narrow tunnel on the opposite side. ATP is bound inside the hole, and L-lysine is bound at the entrance of the tunnel. The conserved Asp36 in the PP-motif coordinates Mg2+. In these initial binding modes, the ATP, Mg2+, and L-lysine are held far apart from each other, but they seem to be brought together for the reaction upon cytidine binding, with putative structural changes of the complex

Publisher: Elsevier Ltd.
Year: 2007
DOI identifier: 10.1016/j.str.2007.09.020
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