Molecular Motors Movies and Images

These movies and images can be used for teaching purposes.  Please acknowledge the source as the Vale Lab web site or iBioSeminars.Org.

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iBio Seminar Clip: The Kinesin Motor - Description of kinesin structur and a cartoon diagram of the molecule (1:09)  

 

iBio Seminar Clip: Structural rearrangements in motor proteins - Animation of changes in the protein structur of kinesin and myosin, as a results of the hydrolysis of ATP (3.36)

 
 
Animated model of processive motion by conventional kinesin. Animation prepared by Graham Johnson (http://fivth.com).  
Animated model for myosin based motility. Animation prepared by Graham Johnson (http://fivth.com).
           
 
Ahmet Yildiz gives a talk on Single Molecule Fluorescence.  
Arne Gennerich gives a talk on Optical Trap techniques.
           
 
Yeast cytoplasmic dynein is a processive motor. Single TMR-lableled dynein molecules can be seen moving processively along axonemal microtubules. The data was collected at 0.5 frames/sec and the movie is shown sped up 100x. The size of the movie window is 7.4 x 18.3um.      
           
           

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(Click images for larger)
 
Kinesin: Artistic depiction of kinesisn transporting membranes along microtubules (artwork prepared by Graham Johnson (graham@grahamj.com), modified from cover artwork from the Journal of Cell Biology, November 27, 2000).  
Dynein: Artwork prepared by Graham Johnson (similar to the cover of Science, March 4, 2011). Based upon crystan structure of Carter et al., 2011 but with artistic license to show walking along a microtubule).
       
Kinesin still-image art: a motor carrying a cargo. Cell, 2002.
Artistic rendering of microtubule-based transport: Kinesin still-image of a VW beetle (representing a kinesin motor) carrying cargo. Cell, 2002.
       
Diversity of kinesin superfamily members: Illustration showing the diverse structures of the tail domains of three classes of kinesins (illustration by Graham Johnson (graham@grahamj.com).
The nucleotide core of kinesin, myosin and G proteins: The nucleotide binding pocket of kinesin, myosin and G proteins displays a similar architecture consisting of 5 parllel beta-strands and one anti-parallel strand.
       
Comparison of the dynein and kinesin crystal structures. The first crystal structures of dynein and kinesin were published by Carter et al., 2011, and Kull et al, 1996. Image from Spudich, J.A., Science 2011 331:1143.
Fun artwork depicting axonal transport before we knew the nature of the transport filaments and the motors. Art made by Steve Downing, Stanford medical student.
       
Common Structure of Kinesin and G Proteins. The common core b-strands and helices of kinesin and G proteins are featured in yellow and similar nucleotide binding loops are shown in red.
Model figure depicting in vitro motility developed from studies of the squid giant axon. Motors (kinesin) transporting microtubules across a glass surface, artificial charged beads along microtubules, and membrane organelles along microtubules.
       
The nucleotide binding pocket of kinesin, myosin, and G proteins displays a similar architecture consisting of 5 parallel beta-strands and one anti-parallel strand.
Comparison of the kinesiin and myosin structures reveals a significant similarity that suggests that they are evolutionaarily related.
       
Kinesin moves to the microtubule plus end by the docking and zippering of the neck linker towards the plus end. Ncd, a member of the Kinesin-14 family, has a distinct mechanical element (a coiled coil).
Crystal structure of the Ncd dimer, L11 (which interacts with microtubules and is also a part of the switch 11 region) is disordered.
       
Kinesin moves to the microtubule plus end by the docking and zippering of the neck linker towards the plus end.
Regulation of Kinesin-3. Illustration of a proposed monomer-to-dimer transition of Un104, a member of the kinesin-3 family. (Artwork prepared by Graham Johnson (graham@grahamj.com).
       
The cytoplasmic dynein holoenzyme (speculative structure; at by Graham Johnson) and several of its proposed cell biological functions.
High spacial resolution tracking of quantum dot-labelled dynein. Unlike kinesin, dynein has a variable step size and frequently takes backwards steps.
       
The crystal structure of the microtubule binding domain and a momdel showing the location of this domain relative to the whole motor domain.
Crystal structure of the yeast cytoplasmic dynein motor domain.
       
Model for a dynein structural change conferred by nucleotide binding. A speculataive model based upon the nucleotide-free structure of dynein.    
       
 
Check back for more movies and images!
 
last updated 9/14/12