Sequential Action of ATP-dependent Subunit Conformational Change and Interaction between Helical Protrusions in the Closure of the Built-in Lid of Group II Chaperonins

ATP drives the conformational change of the group II chaperonin from the open lid substrate-binding conformation to the closed lid conformation to encapsulate an unfolded protein in the central cavity. The detailed mechanism of this conformational change remains unknown. To elucidate the intra-ring...

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Detalhes bibliográficos
Main Authors: Kanzaki, Taro, Iizuka, Ryo, Takahashi, Kazunobu, Maki, Kosuke, Masuda, Rie, Sahlan, Muhamad, Yébenes, Hugo, Valpuesta, José M., Oka, Toshihiko, Furutani, Masahiro, Ishii, Noriyuki, Kuwajima, Kunihiro, Yohda, Masafumi
Formato: Artigo
Idioma:Inglês
Publicado em: American Society for Biochemistry and Molecular Biology 2008
Assuntos:
Protein Structure and Folding
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC3259901/
https://ncbi.nlm.nih.gov/pubmed/18854314
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M805303200
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