Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins.
Prefoldin (GimC) is a hexameric molecular chaperone complex built from two related classes of subunits and present in all eukaryotes and archaea. Prefoldin interacts with nascent polypeptide chains and, in vitro, can functionally substitute for the Hsp70 chaperone system in stabilizing non-native proteins for subsequent folding in the central cavity of a chaperonin. Here, we present the crystal structure and characterization of the prefoldin hexamer from the archaeum Methanobacterium thermoautotrophicum. Prefoldin has the appearance of a jellyfish: its body consists of a double beta barrel assembly with six long tentacle-like coiled coils protruding from it. The distal regions of the coiled coils expose hydrophobic patches and are required for multivalent binding of nonnative proteins.
Siegert
R
R
Max-Planck Institut für Biochemie, Am Klopferspitz 18a, D82152 Martinsried, Germany.
Leroux
M R
MR
Scheufler
C
C
Hartl
F U
FU
Moarefi
I
I
D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry*; D003461:Crystallography; D017014:Methanobacterium; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry* / Q000145:classification; D008969:Molecular Sequence Data; D009038:Motion; D010446:Peptide Fragments / Q000737:chemistry; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D017386:Sequence Homology, Amino Acid; D013499:Surface Properties
D019843:Archaeal Proteins; D018832:Molecular Chaperones; D010446:Peptide Fragments; D021122:Protein Subunits; C112806:prefoldin