The amino acid sequence of elongation factor Tu of Escherichia coli. The complete sequence.

摘要: The complete amino acid sequence of elongation factor Tu Escherichia coli has been established by sequencing overlapping cyanogen bromide and tryptic peptides. Sequence analysis peptides was done primarily solid-phase Edman degradation. Elongation is a single chain polypeptide composed 393 acids (Mr = 43,225). Its NH2 terminus blocked with an acetyl group, as determined mass spectroscopy, lysine 56 partially methylated. cysteine residues associated aminoacyl tRNA guanosine nucleotide binding are located at positions 81 137, respectively. Although coded for two genes, the only site microheterogeneity found carboxyl (residue 393), which either glycine or serine. Comparison first 140 G shows strong (31%) homology. In addition, secondary structure calculations predict remarkable conformational similarities between proteins. NH2-terminal region appears to be beta-sheet domains connected exposed, alpha-helical bridge, includes 14-amino segment released limited treatment trypsin. Structural features aminoacyl-tRNA discussed in light other chemical biochemical data.