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CRYSTAL STRUCTURE OF ARCHAEAL PREFOLDIN (GIMC).CRYSTAL STRUCTURE OF ARCHAEAL PREFOLDIN (GIMC).
Structural highlights
FunctionPFDB_METTH Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPrefoldin (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. Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins.,Siegert R, Leroux MR, Scheufler C, Hartl FU, Moarefi I Cell. 2000 Nov 10;103(4):621-32. PMID:11106732[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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