1FYF

CRYSTAL STRUCTURE OF A TRUNCATED FORM OF THREONYL-TRNA SYNTHETASE COMPLEXED WITH A SERYL ADENYLATE ANALOG

Summary for 1FYF

• Entry DOI: 10.2210/pdb1fyf/pdb
• Related: 1EVK 1EVL 1QF6
• Descriptor: THREONYL-TRNA SYNTHETASE, ZINC ION, 5'-O-(N-(L-SERYL)-SULFAMOYL)ADENOSINE, ... (4 entities in total)
• Functional Keywords: amino acid recognition, zinc ion, trna-synthetase, adenylate analog, deletion mutant, ligase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A8M3
• Total number of polymer chains: 2
• Total formula weight: 94447.97

Authors

Sankaranarayanan, R.,Dock-Bregeon, A.C.,Moras, D. (deposition date: 2000-09-29, release date: 2000-12-27, Last modification date: 2024-02-07)

Primary citation

Dock-Bregeon, A.,Sankaranarayanan, R.,Romby, P.,Caillet, J.,Springer, M.,Rees, B.,Francklyn, C.S.,Ehresmann, C.,Moras, D.
Transfer RNA-mediated editing in threonyl-tRNA synthetase. The class II solution to the double discrimination problem.
Cell(Cambridge,Mass.), 103:877-884, 2000

PubMed Abstract: Threonyl-tRNA synthetase, a class II synthetase, uses a unique zinc ion to discriminate against the isosteric valine at the activation step. The crystal structure of the enzyme with an analog of seryl adenylate shows that the noncognate serine cannot be fully discriminated at that step. We show that hydrolysis of the incorrectly formed ser-tRNA(Thr) is performed at a specific site in the N-terminal domain of the enzyme. The present study suggests that both classes of synthetases use effectively the ability of the CCA end of tRNA to switch between a hairpin and a helical conformation for aminoacylation and editing. As a consequence, the editing mechanism of both classes of synthetases can be described as mirror images, as already seen for tRNA binding and amino acid activation.

PubMed: 11136973
DOI: 10.1016/S0092-8674(00)00191-4

Experimental method

X-RAY DIFFRACTION (1.65 Å)