Crystal structure of the kinesin motor domain reveals a structural similarity to myosin

  title={Crystal structure of the kinesin motor domain reveals a structural similarity to myosin},
  author={F. Kull and E. Sablin and R. Lau and R. Fletterick and R. Vale},
  journal={Acta Crystallographica Section A},
Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular Machines
  • J. Cochran
  • Physics, Medicine
  • Biophysical Reviews
  • 2014
This review focuses on kinesIn motor enzymology with special emphasis on the literature that reports the chemistry, structure and physics of several different kinesin superfamily members. Expand
Force generation by kinesin and myosin cytoskeletal motor proteins
Summary Kinesins and myosins hydrolyze ATP, producing force that drives spindle assembly, vesicle transport and muscle contraction. How do motors do this? Here we discuss mechanisms of motor forceExpand
Stabilization of the ADP/Metaphosphate Intermediate during ATP Hydrolysis in Pre-power Stroke Myosin
It is argued that the present mechanism of metaphosphate stabilization is common to the large family of nucleotide-hydrolyzing enzymes, in general, and yields a chemically consistent model for the catalytic strategy of nucleophilic enzymes in general. Expand
Mechanistic investigation of small molecule inhibitors of kinesin-5 and kinesin-6 family members in cancer drug development
The mechanism by which existing Eg5 inhibitors block catalytic activity and the mechanism through which Eg5 develops resistance to these inhibitors are investigated to understand the underlying molecular mechanism of resistance to Eg5 inhibition. Expand
Three Unconventional Kinesins Exhibit Novel Microtubule Interactions:The Characterization of Kar3Cik1, Kar3Vik1, and Nod
This work characterized Nod as a kinesin that regulates microtubule dynamics by binding to the micro Tubule plus end and promoting microtubules polymerization, providing a mechanistic explanation for the polar ejection force observed in vivo. Expand
Kinesin: switch I & II and the motor mechanism.
None of the new structures is a true motor-ATP state, however, probably because conformational changes at the active site of the kinesins require interactions with microtubules to stabilize the movements. Expand
A new look at the microtubule binding patterns of dimeric kinesins.
This work reinvestigated the microtubule binding patterns of dimeric kinesins by cryo-EM and digital 3D reconstruction under different nucleotide conditions and different motor:tubulin ratios, and determined the molecular mass of motor-tubulin complexes by STEM. Expand
Congruent docking of dimeric kinesin and ncd into three-dimensional electron cryomicroscopy maps of microtubule-motor ADP complexes.
The results support the idea that the observed direct interaction between the two heads is important at some stages of the mechanism by which kinesin moves processively along microtubules. Expand
Investigating the mechanism and energy coupling of DNA gyrase
Investigating the M echanism and Energy C oupling o f DNA gyrase C lare V ictoria Sm ith DNA gyrase is the bacterial type II topoisom erase w hich couples the free energy o f A TP hydro lysis to theExpand
Nucleotide-dependent movements of the kinesin motor domain predicted by simulated annealing.
The structure of an ATP-bound kinesin motor domain is predicted and conformational differences relative to the known ADP-bound form of the protein are identified and an allosteric coupling between the nucleotide pocket and the microtubule binding site of kines in the presence of ADP is revealed. Expand