Related Experiment Video
Updated: May 30, 2026

Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers
Published on: May 4, 2022
Structural basis for the allosteric interference of myosin function by reactive thiol region mutations G680A and
Matthias Preller1, Stefanie Bauer, Nancy Adamek
1Institut für Biophysikalische Chemie, Medizinische Hochschule Hannover, Carl-Neuberg-Strasse 1, 30625 Hannover, Germany.
Abstract:
The cold-sensitive single-residue mutation of glycine 680 in the reactive thiol region of Dictyostelium discoideum myosin-2 or the corresponding conserved glycine in other myosin isoforms has been reported to interfere with motor function. Here we present the x-ray structures of myosin motor domain mutants G680A in the absence and presence of nucleotide as well as the apo structure of mutant G680V. Our results show that the Gly-680 mutations lead to uncoupling of the reactive thiol region from the surrounding structural elements. Structural and functional data indicate that the mutations induce the preferential population of a state that resembles the ADP-bound state. Moreover, the Gly-680 mutants display greatly reduced dynamic properties, which appear to be related to the recovery of myosin motor function at elevated temperatures.
More Related Videos
Related Concept Videos
Overview of Myosin Structure and Function
ATP Synthase: Mechanism
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Ligand Binding and Linkage
Mechanical Protein Functions
Activation and Inactivation of G Proteins

