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
AUTHORS (7)
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.
SUPPLEMENTAL MATERIAL
Coming soon ....
REFERENCES (35)
CITATIONS (172)
EXTERNAL LINKS
PlumX Metrics
RECOMMENDATIONS
FAIR ASSESSMENT
Coming soon ....
JUPYTER LAB
Coming soon ....