2byt | pdb_00002byt

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

spinqualitylabelsall models 2byt, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2byt is a 4 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HG, LEU, SO4, ZN Related: 1h3n, 1obc, 1obh, 2bte Resources: FirstGlance, OCA, RCSB, PDBsum, TOPSAN Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aminoacyl tRNA Synthetase

Proteopedia Page Contributors and Editors (what is this?)

OCA