1KP8

Structural Basis for GroEL-assisted Protein Folding from the Crystal Structure of (GroEL-KMgATP)14 at 2.0 A Resolution

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1KP8 の概要

• エントリーDOI: 10.2210/pdb1kp8/pdb
• 関連するPDBエントリー: 1J4Z 1KPO
• 分子名称: groEL protein, SULFATE ION, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: chaperonin, groel, assisted protein folding, chaperone
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm : P0A6F5
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 810229.99

構造登録者

Wang, J. (登録日: 2001-12-30, 公開日: 2003-03-25, 最終更新日: 2024-02-14)

主引用文献

Wang, J.,Boisvert, D.C.
Structural Basis for GroEL-assisted Protein Folding from the Crystal Structure of (GroEL-KMgATP)14 at 2.0 A Resolution
J.Mol.Biol., 327:843-855, 2003

PubMed Abstract: Nucleotide regulates the affinity of the bacterial chaperonin GroEL for protein substrates. GroEL binds protein substrates with high affinity in the absence of ATP and with low affinity in its presence. We report the crystal structure of (GroEL-KMgATP)(14) refined to 2.0 A resolution in which the ATP triphosphate moiety is directly coordinated by both K(+) and Mg(2+). Upon the binding of KMgATP, we observe previously unnoticed domain rotations and a 102 degrees rotation of the apical domain surface helix I. Two major consequences are a large lateral displacement of, and a dramatic reduction of hydrophobicity in, the apical domain surface. These results provide a basis for the nucleotide-dependent regulation of protein substrate binding and suggest a mechanism for GroEL-assisted protein folding by forced unfolding.

PubMed: 12654267
DOI: 10.1016/S0022-2836(03)00184-0

実験手法

X-RAY DIFFRACTION (2 Å)