Gating of β-Barrel Protein Pores, Porins, and Channels: An Old Problem with New Facets

Lauren A. Mayse, Liviu Movileanu

Research output: Contribution to journalReview articlepeer-review

2 Scopus citations

Abstract

β barrels are ubiquitous proteins in the outer membranes of mitochondria, chloroplasts, and Gram-negative bacteria. These transmembrane proteins (TMPs) execute a wide variety of tasks. For example, they can serve as transporters, receptors, membrane-bound enzymes, as well as adhesion, structural, and signaling elements. In addition, multimeric β barrels are common structural scaffolds among many pore-forming toxins. Significant progress has been made in understanding the functional, structural, biochemical, and biophysical features of these robust and versatile proteins. One frequently encountered fundamental trait of all β barrels is their voltage-dependent gating. This process consists of reversible or permanent conformational transitions between a large-conductance, highly permeable open state and a low-conductance, solute-restrictive closed state. Several intrinsic molecular mechanisms and environmental factors modulate this universal property of β barrels. This review article outlines the typical signatures of voltage-dependent gating. Moreover, we discuss recent developments leading to a better qualitative understanding of the closure dynamics of these TMPs.

Original languageEnglish (US)
Article number12095
JournalInternational journal of molecular sciences
Volume24
Issue number15
DOIs
StatePublished - Aug 2023

Keywords

  • conformational transitions
  • electrophysiology
  • membrane proteins
  • protein folding
  • single-molecule dynamics

ASJC Scopus subject areas

  • Catalysis
  • Molecular Biology
  • Spectroscopy
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry

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