Article
An intact conformation at the tip of elongation factor G domain IV is functionally important.
FEBS letters - 28 Aug 1998
Martemyanov K A, Yarunin A S, Liljas A, Gudkov A T
Abstract excerpt
Three variants of Thermus thermophilus EF-G with mutations in the loop at the distal end of its domain IV were obtained. The replacement of His-573 by Ala and double mutation H573A/D576A did not influence the functional activity of EF-G. On the other hand, the insertion of six amino acids into th...
Topics
- GTP Phosphohydrolase-Linked Elongation Factors
- Mutation
- Peptide Elongation Factor G
- Peptide Elongation Factors
- Protein Conformation
- Structure-Activity Relationship
- Thermus thermophilus