2bte: Difference between revisions

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[[Image:2bte.gif|left|200px]]
{{Seed}}
[[Image:2bte.png|left|200px]]


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{{STRUCTURE_2bte|  PDB=2bte  |  SCENE=  }}  
{{STRUCTURE_2bte|  PDB=2bte  |  SCENE=  }}  


'''THERMUS THERMOPHILUS LEUCYL-TRNA SYNTHETASE COMPLEXED WITH WITH A TRNALEU TRANSCRIPT IN THE POST-EDITING CONFORMATION AND A POST-TRANSFER EDITING SUBSTRATE ANALOGUE'''
===THERMUS THERMOPHILUS LEUCYL-TRNA SYNTHETASE COMPLEXED WITH WITH A TRNALEU TRANSCRIPT IN THE POST-EDITING CONFORMATION AND A POST-TRANSFER EDITING SUBSTRATE ANALOGUE===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_16155583}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_16155583}}


==About this Structure==
==About this Structure==
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[[Category: Class i aminoacyl-trna synthetase editing]]
[[Category: Class i aminoacyl-trna synthetase editing]]
[[Category: Synthetase]]
[[Category: Synthetase]]
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