1ile
From Proteopedia
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| - | [[Image:1ile.gif|left|200px]] | + | [[Image:1ile.gif|left|200px]] |
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| - | '''ISOLEUCYL-TRNA SYNTHETASE''' | + | {{Structure |
| + | |PDB= 1ile |SIZE=350|CAPTION= <scene name='initialview01'>1ile</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ISOLEUCYL-TRNA SYNTHETASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ILE is a [ | + | 1ILE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ILE OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9554847 9554847] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
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[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
[[Category: rsgi]] | [[Category: rsgi]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:51:51 2008'' |
Revision as of 09:51, 20 March 2008
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| , resolution 2.5Å | |||||||
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| 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 Thu Mar 20 11:51:51 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. | ZN | Aminoacyl-trna synthetase | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic
