Dual stoichiometry and subunit organization in the ClpP1/P2 protease from the cyanobacterium Synechococcus elongatus

The Clp protease is conserved among eubacteria and most eukaryotes, and uses ATP to drive protein substrate unfolding and translocation into a chamber of sequestered proteolytic active sites. To investigate the proteolytic core of the ClpXP1/P2 protease from the cyanobacterium Synechococcus elongatu...

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Detalles Bibliográficos
Autores principales: Mikhailov, Victor A., Ståhlberg, Frida, Clarke, Adrian K., Robinson, Carol V.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Academic Press 2015
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4673316/
https://www.ncbi.nlm.nih.gov/pubmed/26525362
http://dx.doi.org/10.1016/j.jsb.2015.10.016

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4673316/
https://www.ncbi.nlm.nih.gov/pubmed/26525362
http://dx.doi.org/10.1016/j.jsb.2015.10.016

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