1FXK
CRYSTAL STRUCTURE OF ARCHAEAL PREFOLDIN (GIMC).
Summary for 1FXK
| Entry DOI | 10.2210/pdb1fxk/pdb |
| Descriptor | PREFOLDIN, PROTEIN (PREFOLDIN), ... (4 entities in total) |
| Functional Keywords | archaeal protein, chaperone |
| Biological source | Methanothermobacter thermautotrophicus More |
| Total number of polymer chains | 3 |
| Total formula weight | 39885.92 |
| Authors | Siegert, R.,Scheufler, C.,Moarefi, I. (deposition date: 2000-09-26, release date: 2000-12-06, Last modification date: 2024-10-30) |
| Primary citation | Siegert, R.,Leroux, M.R.,Scheufler, C.,Hartl, F.U.,Moarefi, I. Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins. Cell(Cambridge,Mass.), 103:621-632, 2000 Cited by PubMed Abstract: 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. PubMed: 11106732DOI: 10.1016/S0092-8674(00)00165-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
Download full validation report
