Affinity Labeling of the GDP/GTP Binding Site in Thermus Thermophilus Elongation Factor Tu
There is a high homology in the folding of the structural domains in both proteins.
The loop region connecting helix A with the β-sheet b (La Cour et al., 1985) of elongation factor Tu is placed in the vicinity of the bound GDP/GTP and in analogy to p21 it probably forms a part of a binding pocket for the nucleotide. This loop corresponds to the “effector loop” of G-proteins.
Cleavage at position 59 of EF-Tu leads to a conformational change resulting in altered reactivity of GDPOXI. towards lysine residues adjacent to the nucleotide binding pocket.
KeywordsLysine Residue Elongation Factor Nucleotide Binding Site Cyanogen Bromide Additional Amino Acid
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