Abstract:
:The guanine nucleotide exchange reaction catalyzed by elongation factor Ts is proposed to arise from the intrusion of the side chains of D80 and F81 near the Mg2+ binding site in EF-Tu. D80A and F81A mutants of E. coli EF-Ts were 2-3-fold less active in promoting GDP exchange with E. coli EF-Tu while the D80AF81A mutant was nearly 10-fold less active. The D84 and F85 mutants of EF-Tsmt were 5-10-fold less active in stimulating the activity of EF-Tumt. The double mutation completely abolished the activity of EF-Tsmt.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Zhang Y,Li X,Spremulli LLdoi
10.1016/0014-5793(96)00789-2subject
Has Abstractpub_date
1996-08-12 00:00:00pages
330-2issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(96)00789-2journal_volume
391pub_type
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