Abstract
The three-dimensional structure of the amino-terminal 44K ATPase fragment of the 70K bovine heat-shock cognate protein has been solved to a resolution of 2.2 Å. The ATPase fragment has two structural lobes with a deep cleft between them; ATP binds at the base of the cleft. Surprisingly, the nucleotide-binding 'core' of the ATPase fragment has a tertiary structure similar to that of hexokinase, although the remainder of the structures of the two proteins are completely dissimilar, suggesting that both the phosphotransferase mechanism and the substrate-induced conformational change intrinsic to the hexokinases may be used by the 70K heat shock-related proteins.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Ellis, R. J., van der Vies, S. M. & Hemmingsen, S. M. Biochem. Soc. Symp. 55, 145–153 (1989).
Bardwell, J. C. & Craig, E. A. Proc. natn. Acad. Sci. U.S.A. 81, 848–852 (1984).
Amir-Shapira, D., Leustek, T., Dalie, B., Weissbach, H. & Brot, N. Proc. natn. Acad. Sci. U.S.A. 87, 749–752 (1990).
Marshall, J. S., DeRocher, A. E., Keegstra, K. & Vierling, E. Proc. natn. Acad. Sci. U.S.A. 87, 374–378 (1990).
Craig, E. A. et al. Molec. cell. Biol. 9, 3000–3008 (1989).
Engman, D. M., Kirchhoff, L. V. & Donelson, J. E. Molec. cell Biol. 9, 5163–5168 (1989).
Leustek, T., Dalie, B., Amir-Shapira, D., Brot, N. & Weissbach, H. Proc. natn. Acad. Sci. U.S.A. 86, 7805–7808 (1989).
Ingolia, T. D. & Craig, E. A. Proc. natn. Acad. Sci. U.S.A. 79, 525–529 (1982).
Munro, S. & Pelham, H. R. Cell 46, 291–300 (1986).
Schmid, S. L., Braell, W. A. & Rothmah, J. E. J. biol. Chem. 260, 10057–10062 (1985).
Schlossman, D. M., Schmid, S. L. Braell, W. A. & Rothman, J. E. J. Cell Biol. 99, 723–733 (1984).
Chappell, T. G. et al. Cell 45, 3–13 (1986).
Chirico, W. J., Waters, M. G. & Blobel, G. Nature 332, 805–810 (1988).
Deshaies, T. J., Koch, B. D., Werner-Washburne, M., Craig, E. A. & Schekman, R. Nature 332, 800–805 (1988).
Green, L. A. & Liem, R. K. J. biol. Chem. 264, 15210–15215 (1989).
Haas, I. G. & Wabl, M. Nature 306, 387–389 (1983).
Gething, M.-J., McCammon, K. & Sambrook, J. Cell 46, 939–950 (1986).
Hurtley, S. M., Bole, D. G., Hoover-Litty, H., Helenius, A. & Copeland, C. S. J. Cell Biol. 108, 2117–2126 (1989).
Chappell, T. G., Konforti, B. B., Schmid, S. L. & Rothman, J. E. J. biol. Chem. 262, 746–751 (1987).
Holmgren, A. & Branden, C.-I. Nature 342, 248–251 (1989).
DeLuca-Flaherty, C., Flaherty, K. M., McIntosh, L. J., Bahrami, B. & McKay, D. B. J. molec. Biol. 200, 749–750 (1988).
Brandhuber, B. J., Boone, T., Kenney, W. C. & McKay, D. B. J. biol. Chem. 262, 12306–12308 (1987).
Hanson, J. C., Watenpaugh, K. D., Sieker, L. & Jensen, L. H. Acta crystallogr. A35, 616–621 (1979).
Durbin, R. M. et al. Science 232, 1127–1131 (1986).
Brandhuber, B. J., Allured, V. S., Falbel, T. G. & McKay, D. B. Proteins 3, 146–154 (1988).
Rossmann, M. G. Acta crystallogr. A32, 774–777 (1976).
Wang, B. C. in Meth. Enzym. 90–112 (1985).
Jones, A. J. appl. Crystallogr. 11, 268–272 (1978).
Brunger, A. T., Kuriyan, J. & Karplus, M. Science 235, 458–460 (1985).
Allured, V. S., Collier, R. J., Carroll, S. F. & McKay, D. B. Proc. natn. Acad. Sci. U.S.A. 83, 1320–1324 (1986).
Remington, S. J., Wiegand, B. & Huber, R. J. molec. Biol. 158, 111–152 (1982).
O'Malley, K., Mauron, A., Barchas, J. D. & Kedes, L. Molec cell. Biol. 5, 3476–3483 (1985).
Dayhoff, M. O., Schwartz, R. M. & Orcutt, B. C. in Atlas of Protein Sequence and Structure, Vol. 5, Suppl. 3 (ed. Dayhoff, M. O.) 342–352 (National Biomedical Research Foundation, Silver Spring, Maryland, 1978).
Fletterick, R. J., Bates, D. J. & Steitz, T. A. Proc. natn. Acad. Sci. U.S.A. 72, 38–42 (1975).
Zylicz, M., LeBowitz, J. H., McMacken, R. & Georgopoulos, C. Proc. natn. Acad. Sci. U.S.A. 80, 6431–6435 (1983).
Itikawa, H., Wada, M., Sekine, K. & Fujita, H. Biochemie 71, 1079–1087 (1989).
Hellinga, H. W. & Evans, P. R. Nature 327, 437–439 (1987).
Anderson, C. M., Stenkamp, R. E., McDonald, R. C. & Steitz, T. A. J. molec. Biol. 123, 207–219 (1978).
Schwab, D. A. & Wilson, J. E. Proc. natn. Acad. Sci. U.S.A. 86, 2563–2567 (1989).
Bennett, W. S. J. & Steitz, T. A. J. molec. Biol. 140, 211–230 (1980).
Lesk, A. M. & Hardman, K. D. Science 216, 539–540 (1982).
Lesk, A. M. & Hardman, K. D. Meth. Enzym. 381–390 (1985).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Flaherty, K., DeLuca-Flaherty, C. & McKay, D. Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature 346, 623–628 (1990). https://doi.org/10.1038/346623a0
Issue Date:
DOI: https://doi.org/10.1038/346623a0
This article is cited by
-
A new look at Hsp70 activity in phosphatidylserine-enriched membranes: chaperone-induced quasi-interdigitated lipid phase
Scientific Reports (2023)
-
Human granzyme B binds Plasmodium falciparum Hsp70-x and mediates antiplasmodial activity in vitro
Cell Stress and Chaperones (2023)
-
Can heat shock protein 70 (HSP70) serve as biomarkers in Antarctica for future ocean acidification, warming and salinity stress?
Polar Biology (2022)
-
3-Hydroxykynurenine as a Potential Ligand for Hsp70 Proteins and Its Effects on Drosophila Memory After Heat Shock
Molecular Neurobiology (2022)
-
HSPA6 and its role in cancers and other diseases
Molecular Biology Reports (2022)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.
