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High-fidelity transfers of genetic information in the central dogma can be achieved by a reaction called editing. The crystal structure of an enzyme with editing activity in translation is presented here at 2.5 angstroms resolution. The enzyme, isoleucyl-transfer RNA synthetase, activates not only the cognate substrate L-isoleucine but also the minimally distinct L-valine in the first, aminoacylation step. Then, in a second, "editing" step, the synthetase itself rapidly hydrolyzes only the valylated products. For this two-step substrate selection, a "double-sieve" mechanism has already been proposed. The present crystal structures of the synthetase in complexes with L-isoleucine and L-valine demonstrate that the first sieve is on the aminoacylation domain containing the Rossmann fold, whereas the second, editing sieve exists on a globular beta-barrel domain that protrudes from the aminoacylation domain.

Enzyme structure with two catalytic sites for double-sieve selection of substrate., Nureki O, Vassylyev DG, Tateno M, Shimada A, Nakama T, Fukai S, Konno M, Hendrickson TL, Schimmel P, Yokoyama S, Science. 1998 Apr 24;280(5363):578-82. PMID:9554847

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Categories: Thermus thermophilus | Fukai, S. | Konno, M. | Nakama, T. | Nureki, O. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Schimmel, P. | Shimada, A. | Tateno, M. | Vassylyev, D G. | Yokoyama, S. | Aminoacyl-trna synthetase | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic