2byt
From Proteopedia
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==Overview== | ==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., . | + | 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== | ==About this Structure== | ||
| - | 2BYT is a | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: editing]] | [[Category: editing]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:23:12 2007'' |
Revision as of 12:17, 5 November 2007
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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. Structure known Active Site: AC1. 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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