Cryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure

Junjie Zhang, Boxue Ma, Frank Dimaio, Nicholai R. Douglas, Lukasz A. Joachimiak, David Baker, Judith Frydman, Michael Levitt, Wah Chiu

Research output: Contribution to journalArticle

37 Scopus citations

Abstract

Chaperonins are large ATP-driven molecular machines that mediate cellular protein folding. Group II chaperonins use their "built-in lid" to close their central folding chamber. Here we report the structure of an archaeal group II chaperonin in its prehydrolysis ATP-bound state at subnanometer resolution using single particle cryo-electron microscopy (cryo-EM). Structural comparison of Mm-cpn in ATP-free, ATP-bound, and ATP-hydrolysis states reveals that ATP binding alone causes the chaperonin to close slightly with a ∼45° counterclockwise rotation of the apical domain. The subsequent ATP hydrolysis drives each subunit to rock toward the folding chamber and to close the lid completely. These motions are attributable to the local interactions of specific active site residues with the nucleotide, the tight couplings between the apical and intermediate domains within the subunit, and the aligned interactions between two subunits across the rings. This mechanism of structural changes in response to ATP is entirely different from those found in group I chaperonins.

Original languageEnglish (US)
Pages (from-to)633-639
Number of pages7
JournalStructure
Volume19
Issue number5
DOIs
StatePublished - May 11 2011
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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    Zhang, J., Ma, B., Dimaio, F., Douglas, N. R., Joachimiak, L. A., Baker, D., Frydman, J., Levitt, M., & Chiu, W. (2011). Cryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure. Structure, 19(5), 633-639. https://doi.org/10.1016/j.str.2011.03.005