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TitleCryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure.
Journal, issue, pagesStructure, Vol. 19, Issue 5, Page 633-639, Year 2011
Publish dateMay 11, 2011
AuthorsJunjie Zhang / Boxue Ma / Frank DiMaio / Nicholai R Douglas / Lukasz A Joachimiak / David Baker / Judith Frydman / Michael Levitt / Wah Chiu /
PubMed AbstractChaperonins 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 ...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.
External linksStructure / PubMed:21565698 / PubMed Central
MethodsEM (single particle)
Resolution4.8 - 8.0 Å
Structure data

5258

3j02

EMDB-5258, PDB-3j02:
Lidless D386A Mm-cpn in the pre-hydrolysis ATP-bound state
Method: EM (single particle) / Resolution: 8.0 Å

PDB-3j03:
Lidless Mm-cpn in the closed state with ATP/AlFx
Method: ELECTRON MICROSCOPY / Resolution: 4.8 Å

Source
  • methanococcus maripaludis (archaea)
KeywordsCHAPERONE / Mm-cpn / Chaperonin / ATP-bound / Group II chaperonin / Protein Folding / Single Particle Reconstruction / Methanococcus maripaludis

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