Literature DB >> 10404219

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

O Llorca1, M G Smyth, J L Carrascosa, K R Willison, M Radermacher, S Steinbacher, J M Valpuesta.   

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 A 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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Year:  1999        PMID： 10404219     DOI： 10.1038/10689

Source DB:  PubMed          Journal:  Nat Struct Biol        ISSN： 1072-8368


  23 in total

1.  Eukaryotic chaperonin CCT stabilizes actin and tubulin folding intermediates in open quasi-native conformations.

Authors:  O Llorca; J Martín-Benito; M Ritco-Vonsovici; J Grantham; G M Hynes; K R Willison; J L Carrascosa; J M Valpuesta
Journal:  EMBO J       Date:  2000-11-15       Impact factor: 11.598

2.  Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle.

Authors:  Jose H Pereira; Corie Y Ralston; Nicholai R Douglas; Daniel Meyer; Kelly M Knee; Daniel R Goulet; Jonathan A King; Judith Frydman; Paul D Adams
Journal:  J Biol Chem       Date:  2010-06-23       Impact factor: 5.157

Review 3.  Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets.

Authors:  Christoph Spiess; Anne S Meyer; Stefanie Reissmann; Judith Frydman
Journal:  Trends Cell Biol       Date:  2004-11       Impact factor: 20.808

4.  Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins.

Authors:  Stefanie Reissmann; Charles Parnot; Christopher R Booth; Wah Chiu; Judith Frydman
Journal:  Nat Struct Mol Biol       Date:  2007-04-29       Impact factor: 15.369

Review 5.  Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin.

Authors:  Gabriel M Altschuler; Keith R Willison
Journal:  J R Soc Interface       Date:  2008-12-06       Impact factor: 4.118

6.  Sequential action of ATP-dependent subunit conformational change and interaction between helical protrusions in the closure of the built-in lid of group II chaperonins.

Authors:  Taro Kanzaki; Ryo Iizuka; Kazunobu Takahashi; Kosuke Maki; Rie Masuda; Muhamad Sahlan; Hugo Yébenes; José M Valpuesta; Toshihiko Oka; Masahiro Furutani; Noriyuki Ishii; Kunihiro Kuwajima; Masafumi Yohda
Journal:  J Biol Chem       Date:  2008-10-13       Impact factor: 5.157

7.  The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins.

Authors:  Carien Dekker; S Mark Roe; Elizabeth A McCormack; Fabienne Beuron; Laurence H Pearl; Keith R Willison
Journal:  EMBO J       Date:  2011-06-24       Impact factor: 11.598

Review 8.  Stress genes and proteins in the archaea.

Authors:  A J Macario; M Lange; B K Ahring; E Conway de Macario
Journal:  Microbiol Mol Biol Rev       Date:  1999-12       Impact factor: 11.056

9.  Nested allosteric interactions in the cytoplasmic chaperonin containing TCP-1.

Authors:  G Kafri; K R Willison; A Horovitz
Journal:  Protein Sci       Date:  2001-02       Impact factor: 6.725

10.  Comparative analysis of the protein folding activities of two chaperonin subunits of Thermococcus strain KS-1: the effects of beryllium fluoride.

Authors:  Takao Yoshida; Ryo Iizuka; Keisuke Itami; Takuo Yasunaga; Haruhiko Sakuraba; Toshihisa Ohshima; Masafumi Yohda; Tadashi Maruyama
Journal:  Extremophiles       Date:  2006-10-28       Impact factor: 2.395
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