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PMID:786370

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Citation

Willick, GE and Kay, CM (1976) Circular dichroism study of the interaction of glutamyl-tRNA synthetase with tRNAGlu2. Biochemistry 15:4347-52

Abstract

The interaction of glutamyl-tRNA synthetase with tRNAGlu2 has been studied. The enzyme was purified to apparent homogeneity, and consists of a single chain with a molecular weight of 59 000. The sedimentation coefficient (sdegrees20,w) was found to be 3.7 S and suggests this enzyme is quite asymmetric. The enzyme binds 1 mol of tRNAGlu2 and has a binding constant of 5 X 10(6) M-1 at pH 7.0 in 0.1 M sodium chloride. A circular dichroic study of the interaction under the same solvent conditions implied both the synthetase and tRNAGlu2 underwent a change in conformation as the complex was formed. In the case of the enzyme there appears to be some loss of alpha-helical structure. The tRNAGlu2 results can be interpreted to indicate a change in the conformation of one or more of the helical regions of this molecule. A residue in the anticodon loop, 5-methylaminomethyl-2-thiouridine, has a distinct circular dichroic band at 340 nm in the free tRNAGlu2. As the complex is formed this band is shifted to the blue. This was interpreted to indicate that the enzyme forms a hydrogen bond with this residue in the anticodon loop, with a change in the conformation of the loop possibly also having occured.

Links

PubMed

Keywords

Amino Acids/analysis; Amino Acyl-tRNA Synthetases/metabolism; Binding Sites; Circular Dichroism; Escherichia coli/enzymology; Glutamate-tRNA Ligase/isolation & purification; Glutamate-tRNA Ligase/metabolism; Glutamates; Macromolecular Substances; Nucleic Acid Conformation; Protein Binding; Protein Conformation; RNA, Transfer; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

ECOLI:SYE

enables

GO:0004818: glutamate-tRNA ligase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete


See also

References

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