Calcium Induced Change in Three-Dimensional Structure of Thin Filaments of Rabbit Skeletal Muscle as Revealed by Cryoelectron Microscopy

1994 ◽  
Vol 203 (2) ◽  
pp. 951-958 ◽  
Author(s):  
T. Ishikawa ◽  
T. Wakabayashi
Keyword(s):  
Skeletal Muscle ◽  
Three Dimensional ◽  
Rabbit Skeletal Muscle ◽  
Dimensional Structure ◽  
Cryoelectron Microscopy ◽  
Thin Filaments ◽  
Three Dimensional Structure

Three-Dimensional Structure of Keyhole Limpet Hemocyanin by Cryoelectron Microscopy and Angular Reconstitution

1995 ◽  
Vol 115 (3) ◽  
pp. 226-232 ◽  
Author(s):  
Prakash Dube ◽  
Elena V. Orlova ◽  
Friederich Zemlin ◽  
Marin van Heel ◽  
J.Robin Harris ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Keyhole Limpet Hemocyanin ◽  
Dimensional Structure ◽  
Cryoelectron Microscopy ◽  
Three Dimensional Structure

scholarly journals Three-dimensional Structure of Acanthamoeba castellanii Myosin-IB (MIB) Determined by Cryoelectron Microscopy of Decorated Actin Filaments

1998 ◽  
Vol 141 (1) ◽  
pp. 155-162 ◽  
Author(s):  
James D. Jontes ◽  
E. Michael Ostap ◽  
Thomas D. Pollard ◽  
Ronald A. Milligan
Keyword(s):  
Actin Filaments ◽  
Catalytic Domain ◽  
Three Dimensional ◽  
Acanthamoeba Castellanii ◽  
Dimensional Structure ◽  
Cryoelectron Microscopy ◽  
Tail Domain ◽  
Three Dimensional Structure ◽  
Myosin I ◽  
Carboxy Terminal

The Acanthamoeba castellanii myosin-Is were the first unconventional myosins to be discovered, and the myosin-I class has since been found to be one of the more diverse and abundant classes of the myosin superfamily. We used two-dimensional (2D) crystallization on phospholipid monolayers and negative stain electron microscopy to calculate a projection map of a “classical” myosin-I, Acanthamoeba myosin-IB (MIB), at ∼18 Å resolution. Interpretation of the projection map suggests that the MIB molecules sit upright on the membrane. We also used cryoelectron microscopy and helical image analysis to determine the three-dimensional structure of actin filaments decorated with unphosphorylated (inactive) MIB. The catalytic domain is similar to that of other myosins, whereas the large carboxy-terminal tail domain differs greatly from brush border myosin-I (BBM-I), another member of the myosin-I class. These differences may be relevant to the distinct cellular functions of these two types of myosin-I. The catalytic domain of MIB also attaches to F-actin at a significantly different angle, ∼10°, than BBM-I. Finally, there is evidence that the tails of adjacent MIB molecules interact in both the 2D crystal and in the decorated actin filaments.

scholarly journals Three-dimensional structure of the Z band in a normal mammalian skeletal muscle.

1996 ◽  
Vol 133 (3) ◽  
pp. 571-583 ◽  
Author(s):  
J P Schroeter ◽  
J P Bretaudiere ◽  
R L Sass ◽  
M A Goldstein
Keyword(s):  
Skeletal Muscle ◽  
Cross Sections ◽  
Three Dimensional ◽  
Square Lattice ◽  
Actin Binding ◽  
Dimensional Structure ◽  
Mammalian Skeletal Muscle ◽  
Axial Filament ◽  
Three Dimensional Structure ◽  
Dimensional Reconstruction

The three-dimensional structure of the vertebrate skeletal muscle Z band reflects its function as the muscle component essential for tension transmission between successive sarcomeres. We have investigated this structure as well as that of the nearby I band in a normal, unstimulated mammalian skeletal muscle by tomographic three-dimensional reconstruction from electron micrograph tilt series of sectioned tissue. The three-dimensional Z band structure consists of interdigitating axial filaments from opposite sarcomeres connected every 18 +/- 12 nm (mean +/- SD) to one to four cross-connecting Z-filaments are observed to meet the axial filaments in a fourfold symmetric arrangement. The substantial variation in the spacing between cross-connecting Z-filament to axial filament connection points suggests that the structure of the Z band is not determined solely by the arrangement of alpha-actinin to actin-binding sites along the axial filament. The cross-connecting filaments bind to or form a "relaxed interconnecting body" halfway between the axial filaments. This filamentous body is parallel to the Z band axial filaments and is observed to play an essential role in generating the small square lattice pattern seen in electron micrographs of unstimulated muscle cross sections. This structure is absent in cross section of the Z band from muscles fixed in rigor or in tetanus, suggesting that the Z band lattice must undergo dynamic rearrangement concomitant with crossbridge binding in the A band.

Three-dimensional structure of the complex between calmodulin mutant lacking the c-terminal five residues and the calmodulin-binding peptide derived from skeletal muscle myosin light-chain kinase

2017 ◽  
Vol 39 (3) ◽  
pp. 309-319
Author(s):  
Vu Van Dung ◽  
Yoshitaka Umetsu ◽  
Shinya Ohki
Keyword(s):  
Skeletal Muscle ◽  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Skeletal Muscle Myosin ◽  
Three Dimensional Structure ◽  
Calmodulin Binding ◽  
Muscle Myosin

In our previous study, functional ability and conformational stability had been examined for C-terminal deletion mutants of a 148-residue Ca2+-binding protein, chicken calmodulin (CaM). In that study, we had reported that a mutant named CCMΔ5, missing five residues at the C-terminus, activates CaM-target as much as full-length CaM does. This finding is intriguing because CCMΔ5 lacks the key residues, Met144 and Met145, for the target activation. To uncover why CCMΔ5 displays proper function, here we report the three-dimensional structure of CCMΔ5 bound to the peptide derived from skeletal muscle myosin light-chain kinase (skMLCK). The structure determination was achieved using multidimensional nuclear magnetic resonance (NMR) spectroscopy. The complex structure of CCM∆5-skMLCK was compared to that of wild CaM-skMLCK. The results showed that the orientation of helix-1 and helix-5 in CCM∆5 differs from those in wild CaM. Moreover, distinctive hydrophobic interaction manner was found in the binding between CCM∆5 and peptide; Phe141, Ala128, Met109, Leu105 and Phe92 of CCM∆5 contribute to the interaction with Trp4 of the skMLCK peptide.   Abbreviations: CaM, calmodulin; CCMΔX, a deletion mutant of CaM that lacks X C-terminal residues; NMR, Nuclear magnetic resonance; PDB, Protein date bank; skMLCK, skeletal muscle myosin light-chain kinase; TOF-MS, Time-of-flight mass spectrometry; RMSD, root mean square deviation; SDS-PAGE, Sodium dodecyl sulfate polyacrylamide gel electrophoresis Citation: Vu Van Dung, Umetsu Y., Ohki S., 2017. Three-dimensional structure of the complex between calmodulin mutant lacking the c-terminal five residues and the calmodulin-binding peptide derived from skeletal muscle myosin light-chain kinase. Tap chi Sinh hoc, 39(3): 309-319. DOI: 10.15625/0866-7160/v39n3.10111. *Corresponding author: [email protected] Received 19 June 2017, accepted 20 August 2017 

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