Structural studies on myosin II: communication between distant protein domains.
Understanding how chemical energy is converted into directed movement is a fundamental problem in biology. In higher organisms this is accomplished through the hydrolysis of ATP by three families of motor proteins: myosin, dynein and kinesin. The most abundant of these is myosin, which operates against actin and plays a central role in muscle contraction. As summarized here, great progress has been made towards understanding the molecular basis of movement through the determination of the three-dimensional structures of myosin and actin and through the establishment of systems for site-directed mutagenesis of this motor protein. It now appears that the generation of movement is coupled to ATP hydrolysis by a series of domain movements within myosin.
Gulick
A M
AM
Institute for Enzyme Research, University of Wisconsin, Madison 53705, USA.
Rayment
I
I
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001696:Biomechanical Phenomena; D002645:Chickens; D004023:Dictyostelium / Q000737:chemistry / Q000235:genetics; D005656:Fungal Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D006868:Hydrolysis; D008958:Models, Molecular; D009038:Motion; D016297:Mutagenesis, Site-Directed; D009218:Myosins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D011487:Protein Conformation; D015800:Protozoan Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D013329:Structure-Activity Relationship
D005656:Fungal Proteins; D015800:Protozoan Proteins; D000255:Adenosine Triphosphate; D009218:Myosins