Refined Model of the 10S Conformation of Smooth Muscle Myosin by Cryo-electron Microscopy 3D Image Reconstruction

2003 ◽  
Vol 329 (5) ◽  
pp. 963-972 ◽  
Author(s):  
Jun Liu ◽  
Thomas Wendt ◽  
Dianne Taylor ◽  
Kenneth Taylor
2021 ◽  
Vol 224 ◽  
pp. 113234
Author(s):  
J.P.J. Chen ◽  
K.E. Schmidt ◽  
J.C.H. Spence ◽  
R.A. Kirian

1998 ◽  
Vol 4 (S2) ◽  
pp. 948-949
Author(s):  
X. Yan ◽  
N. H. Olson ◽  
J. L. Van Etten ◽  
T. S. Baker

Paramecium bursaria Chlorella virus l(PBCV-l), the type species of the Pycodnaviridae family, is a large, plaque-forming virus that replicates in certain unicellular, exsymbiotic, Chlorella-like green algae. The virion (∼lxl09 daltons) has a 330,740 base pair dsDNA genome encapsulated within an icosahedral shell of ∼190nm diameter. Purified virions contain more than 50 different proteins, which account for 65% of the total virion mass and range in size from 10 to more than 200kDa. Vp54, the major capsid protein (40% of total virion protein) is a myristilated glycoprotein but it is not phosphorylated. Three other proteins are located on the virus surface. Virions contain 5-10% lipid, located inside the glycoprotein shell, which is required for virus infectivity. Little is known about the detailed ultrastructure of PBCV-1 virions, though some information has been obtained with sectioned, negatively-stained, and metal-shadowed specimens. We have used cryo-electron microscopy and three-dimensional (3D) image reconstruction methods to examine the native morphology of PBCV-1.


2020 ◽  
Vol 117 (27) ◽  
pp. 15666-15672
Author(s):  
Xiong Liu ◽  
Shi Shu ◽  
Edward D. Korn

Muscle contraction depends on the cyclical interaction of myosin and actin filaments. Therefore, it is important to understand the mechanisms of polymerization and depolymerization of muscle myosins. Muscle myosin 2 monomers exist in two states: one with a folded tail that interacts with the heads (10S) and one with an unfolded tail (6S). It has been thought that only unfolded monomers assemble into bipolar and side-polar (smooth muscle myosin) filaments. We now show by electron microscopy that, after 4 s of polymerization in vitro in both the presence (smooth muscle myosin) and absence of ATP, skeletal, cardiac, and smooth muscle myosins form tail-folded monomers without tail–head interaction, tail-folded antiparallel dimers, tail-folded antiparallel tetramers, unfolded bipolar tetramers, and small filaments. After 4 h, the myosins form thick bipolar and, for smooth muscle myosin, side-polar filaments. Nonphosphorylated smooth muscle myosin polymerizes in the presence of ATP but with a higher critical concentration than in the absence of ATP and forms only bipolar filaments with bare zones. Partial depolymerization in vitro of nonphosphorylated smooth muscle myosin filaments by the addition of MgATP is the reverse of polymerization.


Viruses ◽  
2017 ◽  
Vol 9 (11) ◽  
pp. 321 ◽  
Author(s):  
Nikéa Pittman ◽  
Adam Misseldine ◽  
Lorena Geilen ◽  
Sujata Halder ◽  
J. Smith ◽  
...  

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