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Properties and role of tryptophan residues in the polypeptide chain of elongation factor G from E. coliстатья
- Авторы: Kashparov I.A., Semisotnov G.V., Alakhov Iu B.
- Журнал: Biokhimii∎a (Moscow, Russia)
- Том: 46
- Номер: 8
- Год издания: 1981
- Издательство: IZDATELSTVO NAUKA
- Местоположение издательства: LENINGRADSKOE OTDELENIE MAKAROVA D4, STPETERSBURG, RUSSIA
- Первая страница: 1488
- Последняя страница: 1498
- Аннотация: Using chemical modification and spectrofluorimetry, it was shown that two tryptophane residues of the elongation factor G (EF-G) in positions 51 and 71 from the N-terminus are located on the surface of the EF-G molecule. The tryptophane residue in position 71 is effectively shielded against modification at binding of EF-G guanyl nucleotides. Modification of these tryptophane residues does not result in a loss of the nucleotide-binding activity but completely inhibits EF-G binding to the ribosome. Polarized fluorescence study showed that the relaxation properties of these exposed tryptophane residues essentially depend both on the presence of the C-terminal domain and on binding of nucleotides in the nucleotide-binding site located in the N-terminal part of EF-G. It was assumed that the C-terminal domain, the nucleotide-binding site and the site responsible for the EF-G binding to the ribosome are brought together in the three-dimensional structure of the elongation factor G.
- Добавил в систему: Семисотнов Геннадий Васильевич