1ILE

ISOLEUCYL-TRNA SYNTHETASE

Summary for 1ILE

• Entry DOI: 10.2210/pdb1ile/pdb
• Descriptor: ISOLEUCYL-TRNA SYNTHETASE, ZINC ION (3 entities in total)
• Functional Keywords: aminoacyl-trna synthetase, riken structural genomics/proteomics initiative, rsgi, structural genomics
• Biological source: Thermus thermophilus
• Cellular location: Cytoplasm: P56690
• Total number of polymer chains: 1
• Total formula weight: 94812.83

Authors

Nureki, O.,Vassylyev, D.G.,Tateno, M.,Shimada, A.,Nakama, T.,Fukai, S.,Konno, M.,Schimmel, P.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 1998-02-24, release date: 1999-04-13, Last modification date: 2024-10-30)

Primary citation

Nureki, O.,Vassylyev, D.G.,Tateno, M.,Shimada, A.,Nakama, T.,Fukai, S.,Konno, M.,Hendrickson, T.L.,Schimmel, P.,Yokoyama, S.
Enzyme structure with two catalytic sites for double-sieve selection of substrate.
Science, 280:578-582, 1998

PubMed 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.

PubMed: 9554847
DOI: 10.1126/science.280.5363.578

Experimental method

X-RAY DIFFRACTION (2.5 Å)