Conformational Spread as a Mechanism for Cooperativity in the Bacterial Flagellar Switch

Models, Molecular 0301 basic medicine 570 0303 health sciences Binding Sites Protein Conformation Escherichia coli Proteins Molecular Motor Proteins Membrane Proteins Methyl-Accepting Chemotaxis Proteins 540 Models, Biological Protein Subunits 03 medical and health sciences Allosteric Regulation Bacterial Proteins Flagella Escherichia coli Thermodynamics Monte Carlo Method Protein Binding Signal Transduction
DOI: 10.1126/science.1182105 Publication Date: 2010-02-17T17:27:22Z
ABSTRACT
Complex Cooperativity Cooperativity in multisubunit protein complexes is classically understood in terms of either a concerted model, in which all subunits switch conformation simultaneously, or a sequential model, in which a subunit switches conformation whenever a ligand binds. More recently, a “conformational spread” model has suggested that a conformational coupling between subunits and between subunit and ligand is probabilistic. Using high-resolution optical microscopy, Bai et al. (p. 685 ; see the Perspective by Hilser ) observed multistate switching of the bacterial flagellar switch complex that was previously understood in terms of a concerted allosteric model. The conformational spread model gives quantitative agreement with the data.
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