Hostname: page-component-8448b6f56d-jr42d Total loading time: 0 Render date: 2024-04-23T07:33:45.258Z Has data issue: false hasContentIssue false
  • English
  • Français

Structure and Action of Molecular Tracks and Motors

Published online by Cambridge University Press:  02 July 2020

R.A. Milligan
R.A. Milligan*
Affiliation:
Department of Cell Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA, 92037
Get access

Extract

Molecular motors belonging to the myosin and kinesin superfamilies utilize ATP to move along their respective F-actin and microtubule tracks. The track-motor complexes have not been amenable to crystallization, so x-ray crystallographic investigations have focused on structure determinations of the individual proteins. Although providing detailed descriptions of the structure of each protein, this approach cannot reveal the geometry of interaction of the proteins nor the conformational changes which occur during the mechanochemical cycle. To obtain this information, we use cryoelectron microscopy and image analysis to calculate three dimensional maps of the track-motor complexes at moderate resolution (15-30A) and combine these data with the high resolution x-ray structures to provide near-atomic models of the working assemblies.

We have so far built models of the rigor (nucleotide-free) and ADP actomyosin complexes. In smooth muscle myosin II (a collaboration with H.L. Sweeney, U. Perm.) and brush border myosin I (BBMI), the motor domain of the myosin head is similar in both biochemical states.

Type
High Resolution Protein Structures from Electron Crystallography
Information
Microscopy and Microanalysis , Volume 4 , Issue S2: Proceedings: Microscopy & Microanalysis '98, Microscopy Society of America 56th Annual Meeting, Microbeam Analysis Society 32nd Annual Meeting, Atlanta, Georgia July 12-16, 1998 , July 1998 , pp. 456 - 457
Copyright
Copyright © Microscopy Society of America

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

1. Kabsch, W. et al., Nature 347 (1990) 37.CrossRefGoogle Scholar

2. Rayment, I. et al., Science 261 (1993) 50.CrossRefGoogle Scholar

3. Kull, F.J. et al., Nature 380 (1996) 550.CrossRefGoogle Scholar

4. Sablin, E.P. et al., Nature 380 (1996) 555.CrossRefGoogle Scholar

5. Sack, S. et al., Biochemistry 36 (1997) 16155.CrossRefGoogle Scholar

6. Kozielski, F. et al., Cell 91 (1997) 985.CrossRefGoogle Scholar

7. Rayment, I. et al., Science 261 (1993) 58.CrossRefGoogle Scholar

8. Whittaker, M. et al., Nature 378 (1995) 748.CrossRefGoogle Scholar

9. Jontes, J.D. et al., Nature 378 (1995) 751.CrossRefGoogle Scholar

10. Sosaet, H. al., Cell 90 (1997) 217.Google Scholar

11. Hoenger, A. and Milligan, R.A.. J. Mol. Biol. 265 (1997) 553.CrossRefGoogle Scholar

12. Nogales, E. et al., Nature 391 (1998) 199.CrossRefGoogle Scholar

13. This research was supported by grants from the National Institutes of Health (AR39155, AR44278 and GM52468).Google Scholar