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

Llorca, O., Smyth, M. G., Carrascosa, J. L., Willison, K. R., Radermacher, M., Steinbacher, S., et al. (1999). 3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin. Nature structural biology, 6(7), 639-642. doi:10.1038/10689.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0007-EB37-3 Version Permalink: https://hdl.handle.net/21.11116/0000-0007-EB38-2
Genre: Journal Article

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 Creators:
Llorca, Oscar1, Author
Smyth, Martin G.1, Author
Carrascosa, José L.1, Author
Willison, Keith R. 2, Author
Radermacher, Michael3, Author           
Steinbacher, Stefan4, Author           
Valpuesta, José M. 1, Author
Affiliations:
1Centro Nacional de Biotecnología, CSIC, Campus Universidad Autónoma de Madrid, Spain., ou_persistent22              
2CRC Centre for Cell and Molecular Biology, Institute of Cancer Research, Chester Beatty Laboratories, 237 Fulham Road, Chelsea, SW3 6JB, London, U.K., ou_persistent22              
3Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
4Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              

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 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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Language(s): eng - English
 Dates: 1999-01-111999-03-311999-07-01
 Publication Status: Issued
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/10689
PMID: 10404219
 Degree: -

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Title: Nature structural biology
Source Genre: Journal
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Publ. Info: New York, NY : Nature Pub. Co.
Pages: - Volume / Issue: 6 (7) Sequence Number: - Start / End Page: 639 - 642 Identifier: ISSN: 1072-8368
CoNE: https://pure.mpg.de/cone/journals/resource/111073404672000