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Identification of an allosteric network that influences assembly and function of group II chaperonins

Nature Structural & Molecular Biology volume 24, pages 683–684 (2017)Cite this article

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Group II chaperonins facilitate protein folding by undergoing ATP-driven conformational changes. A recent study reveals a tunable allosteric network in group II chaperonins that includes a residue at the intersubunit interface, which is important for assembly and allosteric coordination. The authors also propose that lower cooperativity allows group II chaperonins to achieve optimal substrate folding over a broad range of ATP concentrations.

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Figure 1: Effects of Met47 mutation in group II chaperonin Cpn.

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Authors and Affiliations

  1. the National Center for Protein Science Shanghai, State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, University of Chinese Academy of Sciences and Shanghai Science Research Center, CAS, Shanghai, China

    Mingliang Jin & Yao Cong

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  1. Mingliang Jin
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  2. Yao Cong
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Correspondence to Yao Cong.

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The authors declare no competing financial interests.

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Jin, M., Cong, Y. Identification of an allosteric network that influences assembly and function of group II chaperonins. Nat Struct Mol Biol 24, 683–684 (2017). https://doi.org/10.1038/nsmb.3459

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