1ile
From Proteopedia
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|PDB= 1ile |SIZE=350|CAPTION= <scene name='initialview01'>1ile</scene>, resolution 2.5Å | |PDB= 1ile |SIZE=350|CAPTION= <scene name='initialview01'>1ile</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ile FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ile OCA], [http://www.ebi.ac.uk/pdbsum/1ile PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ile RCSB]</span> | ||
}} | }} | ||
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[[Category: Vassylyev, D G.]] | [[Category: Vassylyev, D G.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
| - | [[Category: ZN]] | ||
[[Category: aminoacyl-trna synthetase]] | [[Category: aminoacyl-trna synthetase]] | ||
[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
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[[Category: structural genomic]] | [[Category: structural genomic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:21:21 2008'' |
Revision as of 18:21, 30 March 2008
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| , resolution 2.5Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 21:21:21 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
