1ile: Difference between revisions
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'''ISOLEUCYL-TRNA SYNTHETASE''' | '''ISOLEUCYL-TRNA SYNTHETASE''' | ||
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[[Category: Vassylyev, D G.]] | [[Category: Vassylyev, D G.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
[[Category: | [[Category: Aminoacyl-trna synthetase]] | ||
[[Category: | [[Category: Riken structural genomics/proteomics initiative]] | ||
[[Category: | [[Category: Rsgi]] | ||
[[Category: | [[Category: Structural genomic]] | ||
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Revision as of 20:07, 2 May 2008
ISOLEUCYL-TRNA SYNTHETASE
OverviewOverview
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.
About this StructureAbout this Structure
1ILE is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Fri May 2 20:07:28 2008
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Single protein
- 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