We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Enzyme structure with two catalytic sites for double-sieve selection of substrate.
- Authors
Nureki, O; Vassylyev, D G; Tateno, M; Shimada, A; Nakama, T; Fukai, S; Konno, M; Hendrickson, T L; Schimmel, P; Yokoyama, S
- Abstract
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.
- Publication
Science (New York, N.Y.), 1998, Vol 280, Issue 5363, p578
- ISSN
0036-8075
- Publication type
Journal Article
- DOI
10.1126/science.280.5363.578