1U2M

Crystal Structure of Skp

1U2M の概要

• エントリーDOI: 10.2210/pdb1u2m/pdb
• 分子名称: Histone-like protein HLP-1 (2 entities in total)
• 機能のキーワード: coiled coil, chaperone
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm : P0AEU7
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 48556.27

構造登録者

Walton, T.A.,Sousa, M.C. (登録日: 2004-07-19, 公開日: 2004-08-24, 最終更新日: 2024-11-13)

主引用文献

Walton, T.A.,Sousa, M.C.
Crystal Structure of Skp, a Prefoldin-like Chaperone that Protects Soluble and Membrane Proteins from Aggregation
Mol.Cell, 15:367-374, 2004

PubMed Abstract: The Seventeen Kilodalton Protein (Skp) is a trimeric periplasmic chaperone that assists outer membrane proteins in their folding and insertion into membranes. Here we report the crystal structure of Skp from E. coli. The structure of the Skp trimer resembles a jellyfish with alpha-helical tentacles protruding from a beta barrel body defining a central cavity. The architecture of Skp is unexpectedly similar to that of Prefoldin/GimC, a cytosolic chaperone present in eukaria and archea, that binds unfolded substrates in its central cavity. The ability of Skp to prevent the aggregation of model substrates in vitro is independent of ATP. Skp can interact directly with membrane lipids and lipopolysaccharide (LPS). These interactions are needed for efficient Skp-assisted folding of membrane proteins. We have identified a putative LPS binding site on the outer surface of Skp and propose a model for unfolded substrate binding.

PubMed: 15304217
DOI: 10.1016/j.molcel.2004.07.023

実験手法

X-RAY DIFFRACTION (2.3 Å)