Substitution of aspartic acid-80, a residue involved in coordination of magnesium, weakens the GTP binding and strongly enhances the GTPase of the G domain of elongation factor Tu.
Harmark, K
Substitution of aspartic acid-80, a residue involved in coordination of magnesium, weakens the GTP binding and strongly enhances the GTPase of the G domain of elongation factor Tu. [electronic resource] - Biochemistry Aug 1992 - 7367-72 p. digital
Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
0006-2960
10.1021/bi00147a022 doi
Amino Acid Sequence
Aspartic Acid
Base Sequence
Binding Sites
Edetic Acid--pharmacology
GTP Phosphohydrolase-Linked Elongation Factors--genetics
Guanosine Diphosphate--metabolism
Guanosine Triphosphate--metabolism
Kinetics
Magnesium--metabolism
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed
Oligodeoxyribonucleotides
Peptide Elongation Factor Tu--genetics
Protein Conformation
Substitution of aspartic acid-80, a residue involved in coordination of magnesium, weakens the GTP binding and strongly enhances the GTPase of the G domain of elongation factor Tu. [electronic resource] - Biochemistry Aug 1992 - 7367-72 p. digital
Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
0006-2960
10.1021/bi00147a022 doi
Amino Acid Sequence
Aspartic Acid
Base Sequence
Binding Sites
Edetic Acid--pharmacology
GTP Phosphohydrolase-Linked Elongation Factors--genetics
Guanosine Diphosphate--metabolism
Guanosine Triphosphate--metabolism
Kinetics
Magnesium--metabolism
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed
Oligodeoxyribonucleotides
Peptide Elongation Factor Tu--genetics
Protein Conformation