GroEL-GroES complex / chaperonin ATPase / mitochondrial unfolded protein response / protein import into mitochondrial intermembrane space / virion assembly / chaperone cofactor-dependent protein refolding / positive regulation of interferon-alpha production / isomerase activity / ATP-dependent protein folding chaperone / response to radiation ...GroEL-GroES complex / chaperonin ATPase / mitochondrial unfolded protein response / protein import into mitochondrial intermembrane space / virion assembly / chaperone cofactor-dependent protein refolding / positive regulation of interferon-alpha production / isomerase activity / ATP-dependent protein folding chaperone / response to radiation / positive regulation of interleukin-6 production / positive regulation of type II interferon production / unfolded protein binding / protein folding / positive regulation of T cell activation / protein-folding chaperone binding / response to heat / protein refolding / magnesium ion binding / ATP hydrolysis activity / ATP binding / identical protein binding / membrane / cytosol Similarity search - Function
Journal: Biomedicines / Year: 2021 Title: Structural and Computational Study of the GroEL-Prion Protein Complex. Authors: Aleksandra A Mamchur / Andrei V Moiseenko / Irina S Panina / Igor A Yaroshevich / Sofia S Kudryavtseva / Evgeny B Pichkur / Olga S Sokolova / Vladimir I Muronetz / Tatiana B Stanishneva-Konovalova / Abstract: The molecular chaperone GroEL is designed to promote protein folding and prevent aggregation. However, the interaction between GroEL and the prion protein, PrP, could lead to pathogenic ...The molecular chaperone GroEL is designed to promote protein folding and prevent aggregation. However, the interaction between GroEL and the prion protein, PrP, could lead to pathogenic transformation of the latter to the aggregation-prone PrP form. Here, the molecular basis of the interactions in the GroEL-PrP complex is studied with cryo-EM and molecular dynamics approaches. The obtained cryo-EM structure shows PrP to be bound to several subunits of GroEL at the level of their apical domains. According to MD simulations, the disordered N-domain of PrP forms much more intermolecular contacts with GroEL. Upon binding to the GroEL, the N-domain of PrP begins to form short helices, while the C-domain of PrP exhibits a tendency to unfold its α2-helix. In the absence of the nucleotides in the system, these processes are manifested at the hundred nanoseconds to microsecond timescale.
History
Deposition
Oct 20, 2021
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Header (metadata) release
Dec 1, 2021
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Map release
Dec 1, 2021
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Update
Dec 8, 2021
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Current status
Dec 8, 2021
Processing site: PDBe / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
Type of model: NONE / Details: Initial model generated in Relion with SGD
Final reconstruction
Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 4.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0.8) Details: Final reconstruction was performed on C2-symmetry expanded dataset with the mask encapsulating one of the GroEL rings along with the PrP volume. The other ring density was subjected to particle subtraction. Number images used: 82300
Initial angle assignment
Type: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0.8)
Final angle assignment
Type: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0.8)
Final 3D classification
Number classes: 6 / Software - Name: RELION (ver. 3.0.8) Details: The classification performed on C2-symmetry expanded dataset with the mask encapsulating one of the GroEL rings along with the PrP volume. The other ring density was subjected to particle subtraction.
FSC plot (resolution estimation)
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