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Structural Studies of Lysyl-tRNA Synthetase: Conformational Changes Induced by Substrate Binding

Onesti, Silvia ; Desogus, Gianluigi ; Brevet, Annie ; Chen, Josiane ; Plateau, Pierre ; Blanquet, Sylvain ; Brick, Peter

Biochemistry (Easton), 2000-10, Vol.39 (42), p.12853-12861 [Periódico revisado por pares]

United States: American Chemical Society

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Título:
Structural Studies of Lysyl-tRNA Synthetase: Conformational Changes Induced by Substrate Binding
Autor: Onesti, Silvia ; Desogus, Gianluigi ; Brevet, Annie ; Chen, Josiane ; Plateau, Pierre ; Blanquet, Sylvain ; Brick, Peter
Assuntos: Adenosine Triphosphate ; Adenosine Triphosphate - chemistry ; Adenosine Triphosphate - metabolism ; Binding Sites ; Biochemistry, Molecular Biology ; conformation ; Crystallization ; Crystallography, X-Ray ; Escherichia coli ; Escherichia coli - enzymology ; Isoenzymes ; Isoenzymes - chemistry ; Isoenzymes - metabolism ; Life Sciences ; Lysine ; Lysine - chemistry ; Lysine - metabolism ; Lysine-tRNA Ligase ; Lysine-tRNA Ligase - chemistry ; Lysine-tRNA Ligase - metabolism ; Models, Molecular ; Peptide Fragments ; Peptide Fragments - chemistry ; Peptide Fragments - metabolism ; Protein Conformation ; Protein Structure, Tertiary ; RNA, Transfer ; RNA, Transfer - chemistry ; RNA, Transfer - metabolism ; Substrate Specificity ; tRNA Lys
É parte de: Biochemistry (Easton), 2000-10, Vol.39 (42), p.12853-12861
Notas: This work was supported by a Wellcome Trust Grant (Grant 050370). G.D. is a recipient of a Marie Curie Research Training Fellowship. Synchrotron data collection at Hamburg was supported by a EU/TMR LSF grant.
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Descrição: Lysyl-tRNA synthetase is a member of the class II aminoacyl-tRNA synthetases and catalyses the specific aminoacylation of tRNALys. The crystal structure of the constitutive lysyl-tRNA synthetase (LysS) from Escherichia coli has been determined to 2.7 Å 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 α-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°. The result of these changes is a closing up of the active site upon lysine binding.
Editor: United States: American Chemical Society
Idioma: Inglês

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Structural Studies of Lysyl-tRNA Synthetase: Conformational Changes Induced by Substrate Binding

Onesti, Silvia ; Desogus, Gianluigi ; Brevet, Annie ; Chen, Josiane ; Plateau, Pierre ; Blanquet, Sylvain ; Brick, Peter

United States: American Chemical Society

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