1ile
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1ile.gif|left|200px]] | [[Image:1ile.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1ile", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_1ile| PDB=1ile | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''ISOLEUCYL-TRNA SYNTHETASE''' | '''ISOLEUCYL-TRNA SYNTHETASE''' | ||
| Line 35: | Line 32: | ||
[[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]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:07:28 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 17:07, 2 May 2008
ISOLEUCYL-TRNA SYNTHETASE
Overview
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 Structure
1ILE is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
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
Categories: 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
