Topological constraints and modular structure in the folding and functional motions of GlpG, an intramembrane protease.

ABSTRACT: We investigate the folding of GlpG, an intramembrane protease, using perfectly funneled structure-based models that implicitly account for the absence or presence of the membrane. These two models are used to describe, respectively, folding in detergent micelles and folding within a bilayer, which effectively constrains GlpG's topology in unfolded and partially folded states. Structural free-energy landscape analysis shows that although the presence of multiple folding pathways is an intrinsic property of GlpG's modular functional architecture, the large entropic cost of organizing helical bundles in the absence of the constraining bilayer leads to pathways that backtrack (i.e., local unfolding of previously folded substructures is required when moving from the unfolded to the folded state

SUBMITTER: Schafer NP 

PROVIDER: S-EPMC4776503 | biostudies-literature | 2016 Feb

REPOSITORIES: biostudies-literature