1FXK

CRYSTAL STRUCTURE OF ARCHAEAL PREFOLDIN (GIMC).

1FXK の概要

• エントリーDOI: 10.2210/pdb1fxk/pdb
• 分子名称: PREFOLDIN, PROTEIN (PREFOLDIN), ... (4 entities in total)
• 機能のキーワード: archaeal protein, chaperone
• 由来する生物種: Methanothermobacter thermautotrophicus; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 39885.92

構造登録者

Siegert, R.,Scheufler, C.,Moarefi, I. (登録日: 2000-09-26, 公開日: 2000-12-06, 最終更新日: 2024-10-30)

主引用文献

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

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: 11106732
DOI: 10.1016/S0092-8674(00)00165-3

実験手法

X-RAY DIFFRACTION (2.3 Å)