Article
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.
The Journal of biological chemistry - 12 Dec 2008
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
Abstract excerpt
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 cooperative action of subunits for the conformational change, we constructed Thermococcus chaperonin complexes...
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