1ile
From Proteopedia
(New page: 200px<br /><applet load="1ile" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ile, resolution 2.5Å" /> '''ISOLEUCYL-TRNA SYNTHE...) |
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| - | [[Image:1ile.gif|left|200px]]<br /><applet load="1ile" size=" | + | [[Image:1ile.gif|left|200px]]<br /><applet load="1ile" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ile, resolution 2.5Å" /> | caption="1ile, resolution 2.5Å" /> | ||
'''ISOLEUCYL-TRNA SYNTHETASE'''<br /> | '''ISOLEUCYL-TRNA SYNTHETASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | High-fidelity transfers of genetic information in the central dogma can be | + | 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== | ==About this Structure== | ||
| - | 1ILE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1ILE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ILE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Nakama, T.]] | [[Category: Nakama, T.]] | ||
[[Category: Nureki, O.]] | [[Category: Nureki, O.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Schimmel, P.]] | [[Category: Schimmel, P.]] | ||
[[Category: Shimada, A.]] | [[Category: Shimada, A.]] | ||
[[Category: Tateno, M.]] | [[Category: Tateno, M.]] | ||
| - | [[Category: Vassylyev, D | + | [[Category: Vassylyev, D G.]] |
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:01 2008'' |
Revision as of 11:13, 21 February 2008
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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 with as ligand. 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 Feb 21 13:13:01 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 genomics
