Intrinsic Dynamics of the ClpXP Proteolytic Machine Using Elastic Network Models.

ABSTRACT: ClpXP complex is an ATP-dependent mitochondrial matrix protease that binds, unfolds, translocates, and subsequently degrades specific protein substrates. Its mechanisms of operation are still being debated, and several have been proposed, including the sequential translocation of two residues (SC/2R), six residues (SC/6R), and even long-pass probabilistic models. Therefore, it has been suggested to employ biophysical-computational approaches that can determine the kinetics and thermodynamics of the translocation. In this sense, and based on the apparent inconsistency between structural and functional studies, we propose to apply biophysical approaches based on elastic network models (ENM) to study the intrinsic dynamics of the theoretically most probable hydrolysis mechanism. The proposed

SUBMITTER: Gonzalez-Paz L 

PROVIDER: S-EPMC9979342 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature