Structure of the actin-myosin complex and its implications for muscle contraction.
Muscle contraction consists of a cyclical interaction between myosin and actin driven by the concomitant hydrolysis of adenosine triphosphate (ATP). A model for the rigor complex of F actin and the myosin head was obtained by combining the molecular structures of the individual proteins with the low-resolution electron density maps of the complex derived by cryo-electron microscopy and image analysis. The spatial relation between the ATP binding pocket on myosin and the major contact area on actin suggests a working hypothesis for the crossbridge cycle that is consistent with previous independent structural and biochemical studies.
Rayment
I
I
Department of Biochemistry, University of Wisconsin, Madison 53705.
Holden
H M
HM
Whittaker
M
M
Yohn
C B
CB
Lorenz
M
M
Holmes
K C
KC
Milligan
R A
RA
D000199:Actins / Q000737:chemistry* / Q000378:metabolism; D000205:Actomyosin / Q000737:chemistry* / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D001665:Binding Sites; D007091:Image Processing, Computer-Assisted; D008958:Models, Molecular; D009119:Muscle Contraction; D015879:Myosin Subfragments / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D014961:X-Ray Diffraction
D000199:Actins; D015879:Myosin Subfragments; D000255:Adenosine Triphosphate; D000205:Actomyosin