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- W2522058963 abstract "The interaction between the Heat Shock Proteins 70 and 40 is at the core of the ATPase regulation of the chaperone machinery that maintains protein homeostasis. However, the structural details of the interaction remain elusive and contrasting models have been proposed for the transient Hsp70/Hsp40 complexes. Here we combine molecular simulations based on both coarse-grained and atomistic models with coevolutionary sequence analysis to shed light on this problem by focusing on the bacterial DnaK/DnaJ system. The integration of these complementary approaches resulted in a novel structural model that rationalizes previous experimental observations. We identify an evolutionarily conserved interaction surface formed by helix II of the DnaJ J-domain and a structurally contiguous region of DnaK, involving lobe IIA of the nucleotide binding domain, the inter-domain linker, and the<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mi>β</mml:mi></mml:math>-basket of the substrate binding domain." @default.
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- W2522058963 date "2017-05-12" @default.
- W2522058963 modified "2023-10-04" @default.
- W2522058963 title "Modeling Hsp70/Hsp40 interaction by multi-scale molecular simulations and coevolutionary sequence analysis" @default.
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- W2522058963 doi "https://doi.org/10.7554/elife.23471" @default.
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