Structure determination of the motor domain of yeast kinesin kar3 by x-ray crystallography.
Kinesins are molecular motors that share a common structural core with myosins and G proteins and play diverse roles in organelle transport and cell division and movement. Kinesin motors use the chemical energy derived from ATP hydrolysis to generate force for moving on the microtubule track. The mechanism by which kinesin motors capture the energy from ATP hydrolysis and convert it to a force is not completely known. Structural elements that undergo movement and the force-producing conformational changes of the motor must be identified to elucidate this mechanism. X-ray crystallography is the method of choice for elucidating the structural changes of kinesin motors during ATP hydrolysis.
Park
Hee-Won
HW
Department of Pharcology and Structural Genomics Consortium, University of Toronto, Toronto, ON, Canada.
D000255:Adenosine Triphosphate / Q000737:chemistry; D001331:Automation; D001671:Biochemistry / Q000379:methods*; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D005656:Fungal Proteins / Q000737:chemistry*; D006868:Hydrolysis; D008540:Meiosis; D008869:Microtubule-Associated Proteins / Q000737:chemistry*; D008938:Mitosis; D008968:Molecular Conformation; D010957:Plasmids / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D014961:X-Ray Diffraction; D014965:X-Rays
D005656:Fungal Proteins; C063504:KAR3 protein, S cerevisiae; D008869:Microtubule-Associated Proteins; D029701:Saccharomyces cerevisiae Proteins; D000255:Adenosine Triphosphate