PMID:11041850
| Citation |
Onesti, S, Desogus, G, Brevet, A, Chen, J, Plateau, P, Blanquet, S and Brick, P (2000) Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding. Biochemistry 39:12853-61 |
|---|---|
| Abstract |
Lysyl-tRNA synthetase is a member of the class II aminoacyl-tRNA synthetases and catalyses the specific aminoacylation of tRNA(Lys). The crystal structure of the constitutive lysyl-tRNA synthetase (LysS) from Escherichia coli has been determined to 2.7 A resolution in the unliganded form and in a complex with the lysine substrate. A comparison between the unliganded and lysine-bound structures reveals major conformational changes upon lysine binding. The lysine substrate is involved in a network of hydrogen bonds. Two of these interactions, one between the alpha-amino group and the carbonyl oxygen of Gly 216 and the other between the carboxylate group and the side chain of Arg 262, trigger a subtle and complicated reorganization of the active site, involving the ordering of two loops (residues 215-217 and 444-455), a change in conformation of residues 393-409, and a rotation of a 4-helix bundle domain (located between motif 2 and 3) by 10 degrees. The result of these changes is a closing up of the active site upon lysine binding. |
| Links | |
| Keywords |
Adenosine Triphosphate/chemistry; Adenosine Triphosphate/metabolism; Binding Sites; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Isoenzymes/chemistry; Isoenzymes/metabolism; Lysine/chemistry; Lysine/metabolism; Lysine-tRNA Ligase/chemistry; Lysine-tRNA Ligase/metabolism; Models, Molecular; Peptide Fragments/chemistry; Peptide Fragments/metabolism; Protein Conformation; Protein Structure, Tertiary; RNA, Transfer/chemistry; RNA, Transfer/metabolism; Substrate Specificity |
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