2bte
THERMUS THERMOPHILUS LEUCYL-TRNA SYNTHETASE COMPLEXED WITH WITH A TRNALEU TRANSCRIPT IN THE POST-EDITING CONFORMATION AND A POST-TRANSFER EDITING SUBSTRATE ANALOGUE
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OverviewOverview
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 StructureAbout this Structure
2BTE is a Protein complex structure of sequences from Thermus thermophilus with , , , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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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