4ANI

Structural basis for the intermolecular communication between DnaK and GrpE in the DnaK chaperone system from Geobacillus kaustophilus HTA426

4ANI の概要

• エントリーDOI: 10.2210/pdb4ani/pdb
• 関連するPDBエントリー: 2V7Y
• 分子名称: PROTEIN GRPE, CHAPERONE PROTEIN DNAK (2 entities in total)
• 機能のキーワード: chaperone, chaperone cycle, complementary assay
• 由来する生物種: GEOBACILLUS KAUSTOPHILUS; 詳細
• 細胞内の位置: Cytoplasm (Probable): Q5KWZ6
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 316787.98

構造登録者

Wu, C.-C.,Naveen, V.,Chien, C.-H.,Chang, Y.-W.,Hsiao, C.-D. (登録日: 2012-03-19, 公開日: 2012-05-23, 最終更新日: 2024-05-08)

主引用文献

Wu, C.-C.,Naveen, V.,Chien, C.-H.,Chang, Y.-W.,Hsiao, C.-D.
Crystal Structure of Dnak Protein Complexed with Nucleotide Exchange Factor Grpe in Dnak Chaperone System: Insight Into Intermolecular Communication.
J.Biol.Chem., 287:21461-, 2012

PubMed Abstract: The conserved, ATP-dependent bacterial DnaK chaperones process client substrates with the aid of the co-chaperones DnaJ and GrpE. However, in the absence of structural information, how these proteins communicate with each other cannot be fully delineated. For the study reported here, we solved the crystal structure of a full-length Geobacillus kaustophilus HTA426 GrpE homodimer in complex with a nearly full-length G. kaustophilus HTA426 DnaK that contains the interdomain linker (acting as a pseudo-substrate), and the N-terminal nucleotide-binding and C-terminal substrate-binding domains at 4.1-Å resolution. Each complex contains two DnaKs and two GrpEs, which is a stoichiometry that has not been found before. The long N-terminal GrpE α-helices stabilize the linker of DnaK in the complex. Furthermore, interactions between the DnaK substrate-binding domain and the N-terminal disordered region of GrpE may accelerate substrate release from DnaK. These findings provide molecular mechanisms for substrate binding, processing, and release during the Hsp70 chaperone cycle.

PubMed: 22544739
DOI: 10.1074/JBC.M112.344358

実験手法

X-RAY DIFFRACTION (4.094 Å)