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ATP as effector of inorganic pyrophosphatase of Escherichia coli. Identification of the binding site for ATPстатья
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
- Авторы: Rodina E.V., Vorobyeva N.N., Kurilova S.A., Belenikin M.S., Fedorova N.V., Nazarova T.I.
- Журнал: Biochemistry (Moscow)
- Том: 72
- Номер: 1
- Год издания: 2007
- Издательство: Pleiades Publishing, Ltd
- Местоположение издательства: Road Town, United Kingdom
- Первая страница: 93
- Последняя страница: 99
- DOI: 10.1134/S0006297907010117
- Аннотация: The interaction of Escherichia coli inorganic pyrophosphatase (E-PPase) with effector ATP has been studied. The E-PPase has been chemically modified with the dialdehyde derivative of ATP. It has been established that in the experiment only one molecule of effector ATP is bound to each subunit of the hexameric enzyme. Tryptic digestion of the adenylated protein followed by isolation of a modified peptide by HPLC and its mass-spectrometric identification has showed that it is an amino group of Lys146 that undergoes modification. Molecular docking of ATP to E-PPase indicates that the binding site for effector ATP is located in a cluster of positively charged amino acid residues proposed earlier on the basis of site-directed mutagenesis to participate in binding of effector pyrophosphate. Molecular docking also reveals several other amino acid residues probably involved in the interaction with effectors.
- Добавил в систему: Федорова Наталия Викторовна