Crystal Structures of a Group II Chaperonin Reveal the Open and Closed States Associated with the Protein Folding Cycle

Chaperonins are large protein complexes consisting of two stacked multisubunit rings, which open and close in an ATP-dependent manner to create a protected environment for protein folding. Here, we describe the first crystal structure of a group II chaperonin in an open conformation. We have obtaine...

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Detalhes bibliográficos
Main Authors: Pereira, Jose H., Ralston, Corie Y., Douglas, Nicholai R., Meyer, Daniel, Knee, Kelly M., Goulet, Daniel R., King, Jonathan A., Frydman, Judith, Adams, Paul D.
Formato: Artigo
Idioma:Inglês
Publicado em: American Society for Biochemistry and Molecular Biology 2010
Assuntos:
Protein Structure and Folding
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2934662/
https://ncbi.nlm.nih.gov/pubmed/20573955
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M110.125344
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