Three-dimensional Structure Prediction of the Human LMTK3 Catalytic Domain in DYG-in Conformation

2017 ◽  
Vol 06 (01) ◽  
Author(s):  
Loubna Allam ◽  
Wiame Lakhlili ◽  
Zineb Tarhda ◽  
Jihane Akachar ◽  
Fatima Ghrifi ◽  
...  
Keyword(s):  
Structure Prediction ◽  
Catalytic Domain ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure

scholarly journals RNA-Puzzles: A CASP-like evaluation of RNA three-dimensional structure prediction

RNA ◽  
2012 ◽  
Vol 18 (4) ◽  
pp. 610-625 ◽  
Author(s):  
J. A. Cruz ◽  
M.-F. Blanchet ◽  
M. Boniecki ◽  
J. M. Bujnicki ◽  
S.-J. Chen ◽  
...  
Keyword(s):  
Structure Prediction ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
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.

Cloning, Sequence Analysis and Three-dimensional Structure Prediction of DNA Pol I from Thermophilic Geobacillus sp. MKK Isolated from an Iranian Hot Spring

2007 ◽  
Vol 142 (2) ◽  
pp. 200-208 ◽  
Author(s):  
Mohammad Khalaj-Kondori ◽  
Majid Sadeghizadeh ◽  
Khosro Khajeh ◽  
Hossein Naderi-Manesh ◽  
Ali Mohammad Ahadi ◽  
...  
Keyword(s):  
Sequence Analysis ◽  
Structure Prediction ◽  
Hot Spring ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Pol I
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