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3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin

Abstract

The type II chaperonin CCT (chaperonin containing Tcp-1) of eukaryotic cytosol is a heteromeric 16-mer particle composed of eight different subunits. Three-dimensional reconstructions of apo-CCT and ATP-CCT have been obtained at 28 Å resolution by cryo-electron microscopy. Binding of ATP generates an asymmetric particle; one ring has a slightly different conformation from the apo-CCT ring, while the other has undergone substantial movements in the apical domains. Upon ATP binding the apical domains rotate and point towards the cylinder axis, so that the helical protrusions present at their tips could act as a lid closing the ring cavity.

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Figure 1: Average two-dimensional projections of frozen-hydrated CCT.
Figure 2: Several views of the three-dimensional reconstruction of apo-CCT.
Figure 3: Several views of the three-dimensional reconstruction of ATP-CCT.
Figure 4: Conformational changes in CCT that occur upon ATP binding.
Figure 5: Fitting of the X-ray structure of the thermosome from Thermoplasma acidophilum10 with the three-dimensional reconstruction of the ATP-CCT conformation of this study.

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Acknowledgements

This work was partially supported by grants from the DGICYT (J.M.V) and by a Joint Action between Spain and the United Kingdom (J.H.C.). O.L. is a fellow from the Comunidad Autónoma de Madrid. The UK laboratory is supported by the Cancer Research Campaign (CRC). The help of J.M. Carazo, J. R. Castón, J.J. Fernández, R. Huber, S. Marco, J. Pous and C.O. Sánchez is acknowledged.

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Correspondence to José M. Valpuesta.

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Llorca, O., Smyth, M., Carrascosa, J. et al. 3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin . Nat Struct Mol Biol 6, 639–642 (1999). https://doi.org/10.1038/10689

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