1ile: Difference between revisions

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[[Image:1ile.gif|left|200px]]
{{Seed}}
[[Image:1ile.png|left|200px]]


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{{STRUCTURE_1ile|  PDB=1ile  |  SCENE=  }}  
{{STRUCTURE_1ile|  PDB=1ile  |  SCENE=  }}  


'''ISOLEUCYL-TRNA SYNTHETASE'''
===ISOLEUCYL-TRNA SYNTHETASE===




==Overview==
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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.
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{{ABSTRACT_PUBMED_9554847}}


==About this Structure==
==About this Structure==
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[[Category: Rsgi]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
[[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 Tue Jul 1 13:27:33 2008''

Revision as of 10:27, 1 July 2008

File:1ile.png

Template:STRUCTURE 1ile

ISOLEUCYL-TRNA SYNTHETASE

Template:ABSTRACT PUBMED 9554847

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

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