Structure and dynamics of molecular motors

Current Opinion in Structural Biology

Volumn 7, Issue 2, 1997, Pages 239-246

  Amos, Linda A ^a   Cross, Robert A ^b  

^a MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

^b MARIE CURIE RESEARCH INSTITUTE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; KINESIN; MYOSIN;

ATOMIC PARTICLE; CHEMICAL STRUCTURE; CRYOELECTRON MICROSCOPY; DYNAMICS; KINETICS; MICROTUBULE; NONHUMAN; PRIORITY JOURNAL; REVIEW; SEQUENCE HOMOLOGY;

EID: 0030961727     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(97)80032-2     Document Type: Article

References (58)

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2. ••], showing that the two motor domains are remarkably similar despite their opposite directions of movement. A model is proposed in which kinesin and ncd react in opposite ways to the presence or absence of the cleavable γ-phosphate of ATP.
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13. •] compare 3D maps of F-actin decorated with myosin heads in the presence and absence of Mg-ADP. The C-terminal light chain binding domain was reported to pivot 32° (or 23° in the case of smooth muscle myosin) about the end of the actin-binding domain, which remained unchanged.
14. •].
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19. ••].
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26. Hirose K, Lockhart A, Cross RA, Amos LA: Nucleotide-dependent angular change in kinesin motor domain bound to tubulin. Nature 1995, 376:277-279. 3D electron microscope images of negatively stained specimens show 16-protofilamenl microtubules from cricket sperm, decorated with monomeric kinesin motor domain with variations in bound nucleotide. A small projection from the motor domain appears to be tilted nearer to the microtubule plus end in the nucleotide-free state, as compared with the Mg·ADP-containing state.
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29. Hirose K, Lockhart A, Cross RA, Amos LA: Three-dimensional cryoelectron microscopy of dimeric kinesin and ncd motor domains on microtubules. Proc Natl Acad Sci USA 1996, 93:9539-9544. This paper compares the two oppositely moving double-headed motors in the AMP-PNP state. The attached head of each dimer resembles single-headed kinesin and binds to tubulin in the same way; the positions of the second heads are quite different. These are the first reported structural differences that appear to be relevant to the opposite directions of movement of the two motors. In addition, the connections between pairs of heads allow the approximate positions of both the N and C termini to be identified in an attached head.
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32. ••].
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48. Burgess SA: Rigor and relaxed outer dynein arms in replicas of cryofixed motile flagella. J Mol Biol 1995, 250:52-63. Electron microscope images of thousands of individual freeze-etched flagellar dynein arms are compared by single-particle computer analysis. When ATP is rapidly diluted out, the arms appear to be shifted 12nm away from their relaxed positions. In specimens frozen while active, a proportion of the arms are also in this maximally shifted position, suggesting it is a stage in the kinetic cycle. The remaining arms are either relaxed or in a slightly tilted conformation.
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58. Jon Kull homepage on World Wide Web URL: http://util.ucsf.edu/people/kull/kinesin.html.