1fxk
From Proteopedia
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CRYSTAL STRUCTURE OF ARCHAEAL PREFOLDIN (GIMC).
Overview
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.
About this Structure
1FXK is a Protein complex structure of sequences from Methanothermobacter thermautotrophicus. The following page contains interesting information on the relation of 1FXK with [Chaperones]. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 12:43:49 2008
