Three conformational states of scallop myosin S1
10.1073/pnas.200376897
Crossref journal-article
Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences (341)
Abstract

We have determined the structure of the intact scallop myosin head, containing both the motor domain and the lever arm, in the nucleotide-free state and in the presence of MgADP⋅VO4, corresponding to the transition state. These two new structures, together with the previously determined structure of scallop S1 complexed with MgADP (which we interpret as a detached ATP state), reveal three conformations of an intact S1 obtained from a single isoform. These studies, together with new crystallization results, show how the conformation of the motor depends on the nucleotide content of the active site. The resolution of the two new structures (≈4 Å) is sufficient to establish the relative positions of the subdomains and the overall conformation of the joints within the motor domain as well as the position of the lever arm. Comparison of available crystal structures from different myosin isoforms and truncated constructs in either the nucleotide-free or transition states indicates that the major features within the motor domain are relatively invariant in both these states. In contrast, the position of the lever arm varies significantly between different isoforms. These results indicate that the heavy-chain helix is pliant at the junction between the converter and the lever arm and that factors other than the precise position of the converter can influence the position of the lever arm. It is possible that this pliant junction in the myosin head contributes to the compliance known to be present in the crossbridge.

Authors 3
  1. A. Houdusse (first)
  2. A. G. Szent-Györgyi (additional)
  3. C. Cohen (additional)
References 21 Referenced 279
  1. I Rayment, W R Rypniewski, K Schmidt-Bäse, R Smith, D R Tomchick, M M Benning, D A Winkelmann, G Wesenberg, H M Holden Science 261, 50–58 (1993). (10.1126/science.8316857) / Science by Rayment I (1993)
  2. A J Fisher, C A Smith, J B Thoden, R Smith, K Sutoh, H M Holden, I Rayment Biochemistry 34, 8960–8972 (1995). (10.1021/bi00028a004) / Biochemistry by Fisher A J (1995)
  3. C A Smith, I Rayment Biochemistry 35, 5404–5417 (1996). (10.1021/bi952633+) / Biochemistry by Smith C A (1996)
  4. A M Gulick, C B Bauer, J B Thoden, I Rayment Biochemistry 36, 11619–11628 (1997). (10.1021/bi9712596) / Biochemistry by Gulick A M (1997)
  5. R Dominguez, Y Freyzon, K M Trybus, C Cohen Cell 94, 559–571 (1998). (10.1016/S0092-8674(00)81598-6) / Cell by Dominguez R (1998)
  6. A Houdusse, V N Kalabokis, D Himmel, A G Szent-Györgyi, C Cohen Cell 97, 459–470 (1999). (10.1016/S0092-8674(00)80756-4) / Cell by Houdusse A (1999)
  7. A M Gulick, I Rayment BioEssays 19, 561–569 (1997). (10.1002/bies.950190707) / BioEssays by Gulick A M (1997)
  8. K C Holmes Novartis Found Symp 213, 76–92 (1998). / Novartis Found Symp by Holmes K C (1998)
  9. Z Otwinowski, W Minor Data Collection and Processing, eds L Sawyer, N Isaacs, S Bailey (CRC Daresbury Laboratory, Warrington, U.K.), pp. 59–62 (1993). / Data Collection and Processing by Otwinowski Z (1993)
  10. J Navaza Acta Crystallogr A 50, 157–163 (1994). (10.1107/S0108767393007597) / Acta Crystallogr A by Navaza J (1994)
  11. T A Jones, J-Y Zou, S W Cowan, M Kjeldgaard Acta Crystallogr A 47, 897–904 (1991). / Acta Crystallogr A by Jones T A (1991)
  12. A Houdusse, C Cohen Structure (London) 4, 21–32 (1996). (10.1016/S0969-2126(96)00006-8) / Structure (London) by Houdusse A (1996)
  13. I Rayment, H M Holden, M Whittaker, C B Yohn, M Lorenz, K C Holmes, R A Milligan Science 261, 58–65 (1993). (10.1126/science.8316858) / Science by Rayment I (1993)
  14. E W Taylor J Biol Chem 266, 294–302 (1991). (10.1016/S0021-9258(18)52434-0) / J Biol Chem by Taylor E W (1991)
  15. M Walker, X Z Zhang, W Jiang, J Trinick, H D White Proc Natl Acad Sci USA 96, 465–470 (1999). (10.1073/pnas.96.2.465) / Proc Natl Acad Sci USA by Walker M (1999)
  16. M Whittaker, E M Wilson-Kubalek, J E Smith, L Faust, R A Milligan, H L Sweeney Nature (London) 378, 748–751 (1995). (10.1038/378748a0) / Nature (London) by Whittaker M (1995)
  17. I Dobbie, M Linari, G Piazzesi, M Reconditi, N Koubassova, M Ferenczi, V Lombardi, M Irving Nature (London) 396, 383–387 (1998). (10.1038/24647) / Nature (London) by Dobbie I (1998)
  18. J D Jontes, E M Wilson-Kubalek, R A Milligan Nature (London) 378, 751–753 (1995). (10.1038/378751a0) / Nature (London) by Jontes J D (1995)
  19. C Veigel, L M Coluccio, J D Jontes, J C Sparrow, R A Milligan, J E Molloy Nature (London) 398, 530–533 (1999). (10.1038/19104) / Nature (London) by Veigel C (1999)
  20. A L Wells, A W Lin, L Q Chen, D Safer, S M Cain, T Hasson, B O Carragher, R A Milligan, H L Sweeney Nature (London) 401, 505–508 (1999). (10.1038/46835) / Nature (London) by Wells A L (1999)
  21. M A Geeves Biochem J 294, 1–14 (1991). (10.1042/bj2740001) / Biochem J by Geeves M A (1991)
Dates
Type When
Created 23 years, 1 month ago (July 26, 2002, 10:32 a.m.)
Deposited 3 years, 2 months ago (June 7, 2022, 1:02 a.m.)
Indexed 1 month ago (July 28, 2025, 2:21 a.m.)
Issued 24 years, 10 months ago (Oct. 3, 2000)
Published 24 years, 10 months ago (Oct. 3, 2000)
Published Online 24 years, 10 months ago (Oct. 3, 2000)
Published Print 24 years, 10 months ago (Oct. 10, 2000)
Funders 0

None

@article{Houdusse_2000, title={Three conformational states of scallop myosin S1}, volume={97}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.200376897}, DOI={10.1073/pnas.200376897}, number={21}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Houdusse, A. and Szent-Györgyi, A. G. and Cohen, C.}, year={2000}, month=oct, pages={11238–11243} }