5JTP

The structure of chaperone SecB in complex with unstructured proPhoA binding site e

5JTP の概要

• エントリーDOI: 10.2210/pdb5jtp/pdb
• 関連するPDBエントリー: 5JTL 5JTM 5JTN 5JTO 5JTQ 5JTR
• NMR情報: BMRB: 30084
• 分子名称: Protein-export protein SecB, Alkaline phosphatase (2 entities in total)
• 機能のキーワード: molecular chaperone, chaperone-hydrolase complex, chaperone/hydrolase
• 由来する生物種: Escherichia coli O157:H7; 詳細
• 細胞内の位置: Cytoplasm : P0AG88; Periplasm: P00634
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 78752.22

構造登録者

Huang, C.,Saio, T.,Rossi, P.,Kalodimos, C.G. (登録日: 2016-05-09, 公開日: 2016-08-24, 最終更新日: 2024-05-15)

主引用文献

Huang, C.,Rossi, P.,Saio, T.,Kalodimos, C.G.
Structural basis for the antifolding activity of a molecular chaperone.
Nature, 537:202-206, 2016

PubMed Abstract: Molecular chaperones act on non-native proteins in the cell to prevent their aggregation, premature folding or misfolding. Different chaperones often exert distinct effects, such as acceleration or delay of folding, on client proteins via mechanisms that are poorly understood. Here we report the solution structure of SecB, a chaperone that exhibits strong antifolding activity, in complex with alkaline phosphatase and maltose-binding protein captured in their unfolded states. SecB uses long hydrophobic grooves that run around its disk-like shape to recognize and bind to multiple hydrophobic segments across the length of non-native proteins. The multivalent binding mode results in proteins wrapping around SecB. This unique complex architecture alters the kinetics of protein binding to SecB and confers strong antifolding activity on the chaperone. The data show how the different architectures of chaperones result in distinct binding modes with non-native proteins that ultimately define the activity of the chaperone.

PubMed: 27501151
DOI: 10.1038/nature18965

実験手法

SOLUTION NMR