2byt

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[[Image:2byt.gif|left|200px]]<br />
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[[Image:2byt.gif|left|200px]]<br /><applet load="2byt" size="450" color="white" frame="true" align="right" spinBox="true"
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<applet load="2byt" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2byt, resolution 3.30&Aring;" />
caption="2byt, resolution 3.30&Aring;" />
'''THERMUS THERMOPHILUS LEUCYL-TRNA SYNTHETASE COMPLEXED WITH A TRNALEU TRANSCRIPT IN THE POST-EDITING CONFORMATION'''<br />
'''THERMUS THERMOPHILUS LEUCYL-TRNA SYNTHETASE COMPLEXED WITH A TRNALEU TRANSCRIPT IN THE POST-EDITING CONFORMATION'''<br />
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==About this Structure==
==About this Structure==
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2BYT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with ZN, HG, SO4 and LEU as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BYT OCA].
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2BYT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with ZN, HG, SO4 and LEU as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Hg Binding Site For Chain D'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BYT OCA].
==Reference==
==Reference==
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[[Category: editing]]
[[Category: editing]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 17:53:23 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 19:03:36 2007''

Revision as of 16:53, 18 December 2007


2byt, resolution 3.30Å

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THERMUS THERMOPHILUS LEUCYL-TRNA SYNTHETASE COMPLEXED WITH A TRNALEU TRANSCRIPT IN THE POST-EDITING CONFORMATION

Overview

Leucyl-tRNA synthetase (LeuRS) has a specific post-transfer editing, activity directed against mischarged isoleucine and similar noncognate, amino acids. We describe the post-transfer-editing and product complexes, of Thermus thermophilus LeuRS (LeuRSTT) with tRNA(Leu) at 2.9- to 3.3-A, resolution. In the post-transfer-editing configuration, A76 binds in the, editing active site exactly as previously found for the adenosine moiety, of a small-molecule editing-substrate analog. The 60 C-terminal residues, of LeuRSTT, unseen in previous structures, fold into a compact domain, flexibly linked to the rest of the molecule and interacting with the, G19-C56 tertiary base pair of tRNA(Leu). LeuRS recognition of tRNA(Leu), depends essentially on tRNA shape rather than base-specific interactions., The structures show that considerable domain rotations, notably of the, editing domain, accompany the tRNA-3' end dynamics associated successively, with aminoacylation, post-transfer editing and product release.

About this Structure

2BYT is a Protein complex structure of sequences from Thermus thermophilus with ZN, HG, SO4 and LEU as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

The crystal structure of leucyl-tRNA synthetase complexed with tRNALeu in the post-transfer-editing conformation., Tukalo M, Yaremchuk A, Fukunaga R, Yokoyama S, Cusack S, Nat Struct Mol Biol. 2005 Oct;12(10):923-30. Epub 2005 Sep 11. PMID:16155583

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