Towards an understanding of structure-function relationships of elongation factor Tu.
In light of the recently determined structure of elongation factor Tu, and taking into account chemical studies mapping functional sites, a number of residues have been selected for site-directed mutagenesis studies. Gly94, Gly126, His66, His118, Lys89 and Asp90 have each been point-mutated. Preliminary in vitro characterization data are presented.
Wiborg
O
O
Department of Biostructural Chemistry, Aarhus University, Denmark.
Andersen
C
C
Knudsen
C R
CR
Kristensen
T J
TJ
Clark
B F
BF
D000596:Amino Acids / Q000032:analysis / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D010444:Peptide Elongation Factor Tu / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*; D017354:Point Mutation; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship
D000596:Amino Acids; D010444:Peptide Elongation Factor Tu