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.
In: Nature Structural & Molecular Biology, Vol. 18, No. 1, 01.2011, p. 14-9.Research output: Contribution to journal › Journal article › Research › peer-review
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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