Biomaterial Database

Review: nucleotide-dependent conformational changes of the chaperonin containing TCP-1. 2001

R Melki

Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Avenue de la Terrasse, Gif-sur-Yvette, 91198, France.

Current biochemical and structural studies on the conformational changes induced by the nature of nucleotide bound to the chaperonin containing testis complex polypeptide 1 (CCT) are examined to see how consistent the data are. This exercise suggests that the biochemical and structural data are in good agreement. CCT clearly appears as a folding nano-machine fueled by ATP. A careful comparison of the biochemical and structural data, however, highlights a number of points that remain to be carefully documented in order to better understand the nature of the conformational changes in CCT that yield folded target proteins. Special effort should be made to clearly answer the points listed at the end of this review in order to obtain the dynamic sequence of events yielding folded proteins in the eukaryotic cytoplasm similar to what has been obtained for prokaryotes.

UI	MeSH Term	Description	Entries
D011487	Protein Conformation	The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).	Conformation, Protein,Conformations, Protein,Protein Conformations
D005057	Eukaryotic Cells	Cells of the higher organisms, containing a true nucleus bounded by a nuclear membrane.	Cell, Eukaryotic,Cells, Eukaryotic,Eukaryotic Cell
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000255	Adenosine Triphosphate	An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.	ATP,Adenosine Triphosphate, Calcium Salt,Adenosine Triphosphate, Chromium Salt,Adenosine Triphosphate, Magnesium Salt,Adenosine Triphosphate, Manganese Salt,Adenylpyrophosphate,CaATP,CrATP,Manganese Adenosine Triphosphate,MgATP,MnATP,ATP-MgCl2,Adenosine Triphosphate, Chromium Ammonium Salt,Adenosine Triphosphate, Magnesium Chloride,Atriphos,Chromium Adenosine Triphosphate,Cr(H2O)4 ATP,Magnesium Adenosine Triphosphate,Striadyne,ATP MgCl2
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D017510	Protein Folding	Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.	Protein Folding, Globular,Folding, Globular Protein,Folding, Protein,Foldings, Globular Protein,Foldings, Protein,Globular Protein Folding,Globular Protein Foldings,Protein Foldings,Protein Foldings, Globular
D056404	Chaperonin Containing TCP-1	A group II chaperonin found in eukaryotic CYTOSOL. It is comprised of eight subunits with each subunit encoded by a separate gene. This chaperonin is named after one of its subunits which is a T-COMPLEX REGION-encoded polypeptide.	CCT delta Subunit,Chaperonin CCT,Chaperonin CCT, alpha Subunit,Chaperonin CCT, beta Subunit,Chaperonin CCT, delta Subunit,Chaperonin CCT, epsilon Subunit,Chaperonin CCT, eta Subunit,Chaperonin CCT, gamma Subunit,Chaperonin CCT, theta Subunit,Chaperonin CCT, zeta1 Subunit,Chaperonin CCT, zeta2 Subunit,Chaperonin Containing TCP1, Subunit 1,Chaperonin Containing TCP1, Subunit 2,Chaperonin Containing TCP1, Subunit 3,Chaperonin Containing TCP1, Subunit 4,Chaperonin Containing TCP1, Subunit 5,Chaperonin Containing TCP1, Subunit 6A,Chaperonin Containing TCP1, Subunit 6B,Chaperonin Containing TCP1, Subunit 7,Chaperonin Containing TCP1, Subunit 8,Chaperonin Containing t-Complex Polypeptide,Chaperonin-Containing T-Complex Polypeptide 1,Cytosolic Chaperonin,Cytosolic Molecular Chaperone CCT,Testis Complex Polypeptide 1,t-Complex Polypeptide 1,t-Complex Protein 1,Chaperonin Containing T Complex Polypeptide 1,Chaperonin Containing TCP 1,Chaperonin Containing t Complex Polypeptide,Chaperonin, Cytosolic,t Complex Polypeptide 1,t Complex Protein 1
D018833	Chaperonins	A family of multisubunit protein complexes that form into large cylindrical structures which bind to and encapsulate non-native proteins. Chaperonins utilize the energy of ATP hydrolysis to enhance the efficiency of PROTEIN FOLDING reactions and thereby help proteins reach their functional conformation. The family of chaperonins is split into GROUP I CHAPERONINS, and GROUP II CHAPERONINS, with each group having its own repertoire of protein subunits and subcellular preferences.	Chaperonin,Chaperonin Complex,Chaperonin Complexes,Chaperonin Family,Chaperonin Protein Complex,Complex, Chaperonin