PMID:10319817
| Citation |
Sankaranarayanan, R, Dock-Bregeon, AC, Romby, P, Caillet, J, Springer, M, Rees, B, Ehresmann, C, Ehresmann, B and Moras, D (1999) The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site. Cell 97:371-81 |
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| Abstract |
E. coli threonyl-tRNA synthetase (ThrRS) is a class II enzyme that represses the translation of its own mRNA. We report the crystal structure at 2.9 A resolution of the complex between tRNA(Thr) and ThrRS, whose structural features reveal novel strategies for providing specificity in tRNA selection. These include an amino-terminal domain containing a novel protein fold that makes minor groove contacts with the tRNA acceptor stem. The enzyme induces a large deformation of the anticodon loop, resulting in an interaction between two adjacent anticodon bases, which accounts for their prominent role in tRNA identity and translational regulation. A zinc ion found in the active site is implicated in amino acid recognition/discrimination. |
| Links | |
| Keywords |
Amino Acyl-tRNA Synthetases/chemistry; Amino Acyl-tRNA Synthetases/genetics; Amino Acyl-tRNA Synthetases/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Base Sequence; Binding Sites/genetics; Catalytic Domain; Dimerization; Enzyme Activation/physiology; Escherichia coli/enzymology; Escherichia coli/genetics; Genetic Complementation Test; Molecular Mimicry; Molecular Sequence Data; Nucleic Acid Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; RNA, Messenger/genetics; RNA, Transfer, Amino Acyl/chemistry; RNA, Transfer, Amino Acyl/genetics; RNA, Transfer, Amino Acyl/metabolism; Sequence Homology, Amino Acid; Zinc/chemistry |
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