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Why does mutation of Gln61 in Ras by the nitro analog NGln maintain activity of Ras-GAP in hydrolysis of guanosine triphosphate?статья
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: 22 ноября 2015 г.
- Авторы: Khrenova Maria G., Grigorenko Bella L., Mironov Vladimir A., Nemukhin Alexander V.
- Журнал: Proteins: Structure, Function and Bioinformatics
- Том: 83
- Номер: 11
- Год издания: 2015
- Издательство: Wiley-Liss Inc
- Местоположение издательства: United States
- Первая страница: 2091
- Последняя страница: 2099
- DOI: 10.1002/prot.24927
- Аннотация: Interpretation of the experiments showing that the Ras-GAP protein complex maintains activity in guanosine triphosphate (GTP) hydrolysis upon replacement of Glu61 in Ras with its unnatural nitro analog, NGln, is an important issue for understanding details of chemical transformations at the enzyme active site. By using molecular modeling we demonstrate that both glutamine and its nitro analog in the aci-nitro form participate in the reaction of GTP hydrolysis at the stages of proton transfer and formation of inorganic phosphate. The computed structures and the energy profiles for the complete pathway from the enzyme-substrate to enzyme-product complexes for the wild-type and mutated Ras suggest that the reaction mechanism is not affected by this mutation.
- Добавил в систему: Хренова Мария Григорьевна