Three myosin V structures delineate essential features of chemo-mechanical transduction.
The molecular motor, myosin, undergoes conformational changes in order to convert chemical energy into force production. Based on kinetic and structural considerations, we assert that three crystal forms of the myosin V motor delineate the conformational changes that myosin motors undergo upon detachment from actin. First, a motor domain structure demonstrates that nucleotide-free myosin V adopts a specific state (rigor-like) that is not influenced by crystal packing. A second structure reveals an actomyosin state that favors rapid release of ADP, and differs from the rigor-like state by a P-loop rearrangement. Comparison of these structures with a third structure, a 2.0 angstroms resolution structure of the motor bound to an ATP analog, illuminates the structural features that provide communication between the actin interface and nucleotide-binding site. Paramount among these is a region we name the transducer, which is composed of the seven-stranded beta-sheet and associated loops and linkers. Reminiscent of the beta-sheet distortion of the F1-ATPase, sequential distortion of this transducer region likely controls sequential release of products from the nucleotide pocket during force generation.
Coureux
Pierre-Damien
PD
Structural Motility, Institut Curie CNRS, UMR144, Paris, France.
Sweeney
H Lee
HL
Houdusse
Anne
A
D000199:Actins / Q000737:chemistry; D000255:Adenosine Triphosphate / Q000737:chemistry; D000818:Animals; D001696:Biomechanical Phenomena; D002645:Chickens; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry*; D024701:Myosin Type V / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation
D000199:Actins; D020409:Molecular Motor Proteins; D000255:Adenosine Triphosphate; D024701:Myosin Type V