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- W2007662600 abstract "Proteasome is involved in the degradation of proteins. Proteasome activators bind to the proteasome core particle (CP) and facilitate opening a gate of the CP, where Tyr8 and Asp9 in the N-termini tails of the CP form the ordered open gate. In a double mutant (Tyr8Gly/Asp9Gly), the N-termini tails are disordered and the stabilized open-gate conformation cannot be formed. To understand how proteasome is responsible for the efficient proteolysis of the substrate, four different molecular dynamics (MD) simulations were carried out: ordered- and disordered-gate models of the CP complexed with an ATP-independent PA26 and ordered- and disordered-gate models of the CP complexed with an ATP-dependent PAN-like activator. The free-energies of the translocation of a poly-peptide substrate moving through the gate were estimated using an MD simulation program called SCUBA developed by the Japan Atomic Energy Agency (JAEA). In the ordered-gate models, the substrate in the activator was more stable than that in the CP. The conformational entropy of the N-termini tails of the CP was larger when the substrate was in the activator than in the CP. In the disordered-gate models, the substrate in the activator was more destabilized than in the ordered-gate models. The mutated N-termini tails became randomized and their increased conformational entropy could no longer increase further even when the substrate was in the activator, meaning the randomized N-termini tails had lost the ability to stabilize the substrate in the activator. Thus, it was concluded that the dynamics of the N-termini tails entropically play a key role in the translocation of the substrate." @default.
- W2007662600 created "2016-06-24" @default.
- W2007662600 creator A5053952899 @default.
- W2007662600 date "2015-01-01" @default.
- W2007662600 modified "2023-09-29" @default.
- W2007662600 title "Free-Energy Landscapes of the Translocation of a Substrate in Four Proteasome - Activator Complexes Analyzed using Molecular Dynamics Simulations" @default.
- W2007662600 doi "https://doi.org/10.1016/j.bpj.2014.11.2919" @default.
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