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PMID: 15583139 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Structure of the complex between the cytosolic chaperonin CCT and phosducin-like protein.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 101 ·No. 50 ·2004-12-14 ·Pages 17410-5

Martín-Benito J, Bertrand S, Hu T, Ludtke PJ, McLaughlin JN, Willardson BM, Carrascosa JL, Valpuesta JM

Abstract

The three-dimensional structure of the complex formed between the cytosolic chaperonin CCT (chaperonin containing TCP-1) and phosducin (Pdc)-like protein (PhLP), a regulator of CCT activity, has been solved by cryoelectron microscopy. Binding of PhLP to CCT occurs through only one of the chaperonin rings, and the protein does not occupy the central folding cavity but rather sits above it through interactions with two regions on opposite sides of the ring. This causes the apical domains of the CCT subunits to close in, thus excluding access to the folding cavity. The atomic model of PhLP generated from several atomic structures of the homologous Pdc fits very well with the mass of the complex attributable to PhLP and predicts the involvement of several sequences of PhLP in CCT binding. Binding experiments performed with PhLP/Pdc chimeric proteins, taking advantage of the fact that Pdc does not interact with CCT, confirm that both the N- and C-terminal domains of PhLP are involved in CCT binding and that several regions suggested by the docking experiment are indeed critical in the interaction with the cytosolic chaperonin.

MeSH Terms
Amino Acid Sequence Animals Carrier Proteins/chemistry,metabolism,ultrastructure Cattle Chaperonin Containing TCP-1 Chaperonins/chemistry,metabolism,ultrastructure Microscopy, Electron Models, Molecular Molecular Chaperones Molecular Sequence Data Multiprotein Complexes/chemistry,metabolism,ultrastructure Nerve Tissue Proteins/chemistry,metabolism,ultrastructure Protein Binding Protein Structure, Quaternary Protein Subunits/chemistry,metabolism Rats Sequence Alignment
Chemicals
Carrier Proteins Molecular Chaperones Multiprotein Complexes Nerve Tissue Proteins Pdcl protein, rat Protein Subunits Chaperonin Containing TCP-1 Chaperonins
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Martín-Benito Jaime
Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas, Campus de la Universidad Autónoma de Madrid, 28049 Madrid, Spain.
Bertrand Sara
Hu Ting
Ludtke Paul J
McLaughlin Joseph N
Willardson Barry M
Carrascosa José L
Valpuesta José M
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.0405070101
Published
2004-12-14
Epub
2004-00-06
Pages
17410-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC536017
Subset
IM
Grants
NEI NIH HHS · R01 EY012287 · United States
NEI NIH HHS · EY 12287 · United States
External Links
PubMed source DOI: 10.1073/pnas.0405070101 PMC Full Text View journal details
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