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Ring separation highlights the protein-folding mechanism used by the phage EL-encoded chaperoninстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 11 апреля 2017 г.
- Авторы: Molugu SK, Hildenbrand ZL, Morgan DG, Sherman MB, He L., Georgopoulos C., Sernova NV, Kurochkina LP, Mesyanzhinov VV, Miroshnikov KA, Bernal RA
- Журнал: Structure
- Том: 24
- Номер: 4
- Год издания: 2016
- Издательство: Cell Press
- Местоположение издательства: United States
- Первая страница: 537
- Последняя страница: 546
- DOI: 10.1016/j.str.2016.02.006.
- Аннотация: Chaperonins are ubiquitous, ATP-dependent protein- folding molecular machines that are essential for all forms of life. Bacteriophage 4EL encodes its own chaperonin to presumably fold exceedingly large viral proteins via profoundly different nucleotide- binding conformations. Our structural investigations indicate that ATP likely binds to both rings simultaneously and that a misfolded substrate acts as the trigger for ATP hydrolysis. More importantly, the 4EL complex dissociates into two single rings resulting from an evolutionarily altered residue in the highly conserved ATP-binding pocket. Conformational changes also more than double the volume of the single-ring internal chamber such that larger viral proteins are accommodated. This is illustrated by the fact that 4EL is capable of folding b-galactosidase, a 116-kDa protein. Collectively, the architecture and protein-folding mechanism of the 4EL chaperonin are significantly different from those observed in group I and II chaperonins.
- Добавил в систему: Курочкина Лидия Петровна