Crystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulin

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Crystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulin. / Muñoz, Inés G; Yébenes, Hugo; Zhou, Min; Mesa, Pablo; Serna, Marina; Park, Ah Young; Bragado-Nilsson, Elisabeth; Beloso, Ana; de Cárcer, Guillermo; Malumbres, Marcos; Robinson, Carol V; Valpuesta, José M; Montoya, Guillermo.

I: Nature Structural & Molecular Biology, Bind 18, Nr. 1, 01.2011, s. 14-9.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Muñoz, IG, Yébenes, H, Zhou, M, Mesa, P, Serna, M, Park, AY, Bragado-Nilsson, E, Beloso, A, de Cárcer, G, Malumbres, M, Robinson, CV, Valpuesta, JM & Montoya, G 2011, 'Crystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulin', Nature Structural & Molecular Biology, bind 18, nr. 1, s. 14-9. https://doi.org/10.1038/nsmb.1971

APA

Muñoz, I. G., Yébenes, H., Zhou, M., Mesa, P., Serna, M., Park, A. Y., Bragado-Nilsson, E., Beloso, A., de Cárcer, G., Malumbres, M., Robinson, C. V., Valpuesta, J. M., & Montoya, G. (2011). Crystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulin. Nature Structural & Molecular Biology, 18(1), 14-9. https://doi.org/10.1038/nsmb.1971

Vancouver

Muñoz IG, Yébenes H, Zhou M, Mesa P, Serna M, Park AY o.a. Crystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulin. Nature Structural & Molecular Biology. 2011 jan.;18(1):14-9. https://doi.org/10.1038/nsmb.1971

Author

Muñoz, Inés G ; Yébenes, Hugo ; Zhou, Min ; Mesa, Pablo ; Serna, Marina ; Park, Ah Young ; Bragado-Nilsson, Elisabeth ; Beloso, Ana ; de Cárcer, Guillermo ; Malumbres, Marcos ; Robinson, Carol V ; Valpuesta, José M ; Montoya, Guillermo. / Crystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulin. I: Nature Structural & Molecular Biology. 2011 ; Bind 18, Nr. 1. s. 14-9.

Bibtex

@article{97408e96ef574305976e9bff66f9f19f,
title = "Crystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulin",
abstract = "Protein folding is assisted by molecular chaperones. CCT (chaperonin containing TCP-1, or TRiC) is a 1-MDa oligomer that is built by two rings comprising eight different 60-kDa subunits. This chaperonin regulates the folding of important proteins including actin, α-tubulin and β-tubulin. We used an electron density map at 5.5 {\AA} resolution to reconstruct CCT, which showed a substrate in the inner cavities of both rings. Here we present the crystal structure of the open conformation of this nanomachine in complex with tubulin, providing information about the mechanism by which it aids tubulin folding. The structure showed that the substrate interacts with loops in the apical and equatorial domains of CCT. The organization of the ATP-binding pockets suggests that the substrate is stretched inside the cavity. Our data provide the basis for understanding the function of this chaperonin.",
keywords = "Animals, Binding Sites, Cattle, Chaperonin Containing TCP-1/chemistry, Crystallography, X-Ray, Mass Spectrometry, Models, Molecular, Protein Folding, Protein Structure, Tertiary, Protein Subunits/chemistry, Tubulin/chemistry",
author = "Mu{\~n}oz, {In{\'e}s G} and Hugo Y{\'e}benes and Min Zhou and Pablo Mesa and Marina Serna and Park, {Ah Young} and Elisabeth Bragado-Nilsson and Ana Beloso and {de C{\'a}rcer}, Guillermo and Marcos Malumbres and Robinson, {Carol V} and Valpuesta, {Jos{\'e} M} and Guillermo Montoya",
year = "2011",
month = jan,
doi = "10.1038/nsmb.1971",
language = "English",
volume = "18",
pages = "14--9",
journal = "Nature Structural and Molecular Biology",
issn = "1545-9993",
publisher = "nature publishing group",
number = "1",

}

RIS

TY - JOUR

T1 - Crystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulin

AU - Muñoz, Inés G

AU - Yébenes, Hugo

AU - Zhou, Min

AU - Mesa, Pablo

AU - Serna, Marina

AU - Park, Ah Young

AU - Bragado-Nilsson, Elisabeth

AU - Beloso, Ana

AU - de Cárcer, Guillermo

AU - Malumbres, Marcos

AU - Robinson, Carol V

AU - Valpuesta, José M

AU - Montoya, Guillermo

PY - 2011/1

Y1 - 2011/1

N2 - Protein folding is assisted by molecular chaperones. CCT (chaperonin containing TCP-1, or TRiC) is a 1-MDa oligomer that is built by two rings comprising eight different 60-kDa subunits. This chaperonin regulates the folding of important proteins including actin, α-tubulin and β-tubulin. We used an electron density map at 5.5 Å resolution to reconstruct CCT, which showed a substrate in the inner cavities of both rings. Here we present the crystal structure of the open conformation of this nanomachine in complex with tubulin, providing information about the mechanism by which it aids tubulin folding. The structure showed that the substrate interacts with loops in the apical and equatorial domains of CCT. The organization of the ATP-binding pockets suggests that the substrate is stretched inside the cavity. Our data provide the basis for understanding the function of this chaperonin.

AB - Protein folding is assisted by molecular chaperones. CCT (chaperonin containing TCP-1, or TRiC) is a 1-MDa oligomer that is built by two rings comprising eight different 60-kDa subunits. This chaperonin regulates the folding of important proteins including actin, α-tubulin and β-tubulin. We used an electron density map at 5.5 Å resolution to reconstruct CCT, which showed a substrate in the inner cavities of both rings. Here we present the crystal structure of the open conformation of this nanomachine in complex with tubulin, providing information about the mechanism by which it aids tubulin folding. The structure showed that the substrate interacts with loops in the apical and equatorial domains of CCT. The organization of the ATP-binding pockets suggests that the substrate is stretched inside the cavity. Our data provide the basis for understanding the function of this chaperonin.

KW - Animals

KW - Binding Sites

KW - Cattle

KW - Chaperonin Containing TCP-1/chemistry

KW - Crystallography, X-Ray

KW - Mass Spectrometry

KW - Models, Molecular

KW - Protein Folding

KW - Protein Structure, Tertiary

KW - Protein Subunits/chemistry

KW - Tubulin/chemistry

U2 - 10.1038/nsmb.1971

DO - 10.1038/nsmb.1971

M3 - Journal article

C2 - 21151115

VL - 18

SP - 14

EP - 19

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

SN - 1545-9993

IS - 1

ER -

ID: 245614630