Abstract
The atomic models of the complex between rabbit skeletal muscle actin and bovine pancreatic deoxyribonuclease I both in the ATP and ADP forms have been determined byo X-ray analysis at an effective resolution of 2.8 Å and 3 Å, respectively. The two structures are very similar. The actin molecule consists of two domains which can be further subdivided into two subdomains. ADP or ATP is located in the cleft between the domains with a calcium ion bound to the β- or β- and γ-phosphates, respectively. The motif of a five-stranded (3 sheet consisting of a (3 meander and a right handed β α β unit appears in each domain suggesting that gene duplication might have occurred. These sheets have the same topology as that found in hexokinase.
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
Straub, F. B. Studies, University of Szeged II, 3–15 (1942).
Straub, F. B. Studies, University of Szeged III, 23–27 (1943).
Pollard, T. D. Curr. Opinion Cell Biol. 2, 33–40 (1990).
Vandekerckhove, J. Curr. Opinion Cell Biol. 2, 41–50 (1990).
Elzinga, M., Collins, J. H., Kuehl, W. M. & Adelstein, R. S. Proc. natn. Acad. Sci. U.S.A. 70, 2687–2691 (1973).
Collins, J. H. & Elzinga, M. J. biol. Chem. 250, 5915–5920 (1975).
Lu, R. C. & Elzinga, M. Biochemistry 16, 5801–5806 (1977).
Vandekerckhove, J. & Weber, K. Eur. J. Biochem. 90, 451–462 (1978).
Lazarides, E. & Lindberg, U. Proc. natn. Acad. Sci. U.S.A. 71, 4742–4746 (1974).
Mannherz, H. G., Barrington-Leigh, J., Leberman, R. & Pfrang, H. FEBS Lett. 60, 34–38 (1975).
Hitchcock, S. E. J. biol. Chem. 255, 5668–5673 (1980).
Mannherz, H. G., Kabsch, W. & Leberman, R. FEBS Lett. 73, 141–143 (1977).
Sugino H. et al. J. Biochem. 86, 257–260 (1979).
Suck, D., Kabsch, W. & Mannherz, H. G. Proc. natn. Acad. Sci. U.S.A. 78, 4319–4323 (1981).
Kabsch, W., Mannherz, H. G. & Suck, D. EMBO J. 4, 2113–2118 (1985).
Suck, D., Oefner, C. & Kabsch, W. EMBO J. 3, 2423–2430 (1984).
Oefner, C. & Suck, D. J. molec. Biol. 192, 605–632 (1986).
Kabsch, W. J. appl. Crystallogr. 21, 916–924 (1988).
Kabsch, W. J. appl. Crystallogr. 21, 67–71 (1988).
Kabsch, W., Pai, E. F., Mannherz, H. G. & Suck, D. Springer Series in Biophysics (eds Aebi U. & Engel, J.) 3, 42–47 (1989).
Bruenger, A. T., Kuriyan, J. & Karplus, M. Science 235, 458–460 (1987).
Read, R. J. Acta crystallogr. A42, 140–149 (1986).
Jones, T. A. J. appl. Crystallogr. 11, 268–272 (1978).
Steitz, T. A., Fletterick, R. J., Anderson, W. A. & Anderson, C. M. J. molec. Biol. 104, 197–222 (1976).
Kabsch, W. & Sander, C. Biopolymers 22, 2577–2637 (1983).
Naharro, G., Robbins, K. C. & Reddy, E. P. Science 223, 63–66 (1984).
Holmes, K. C., Popp, D., Gebhard, W. & Kabsch, W., Nature 347, 44–49 (1990).
Polzar, B., Nowak, E., Goody, R. S. & Mannherz, H. G. Eur. J. Biochem. 182, 267–275 (1989).
Suck, D., Lahm, A. & Oefner, C. Nature 332, 464–468 (1988).
Boyer, M., Roustan, C. & Benyamin, Y. Biosci. Rpt 5, 39–46 (1985).
Sutoh, K. Biochemistry 23, 1942–1946 (1984).
Mornet, D. & Ue, K. Proc. natn. Acad. Sci. U.S.A. 81, 3680–3684 (1984).
Mornet, D., Bonet, A., Audemard, E. & Bonicel, J. J. Muscle Res. Cell Motil. 10, 10–24 (1989).
Jacobson, G. R. & Rosenbusch, J. P. Proc. natn. Acad. Sci. U.S.A. 73, 2742–2746 (1976).
Johnson, P., Wester, P. J. & Hikida, R. S. Biochim. biophys. Acta 578, 253–257 (1979).
Konno, K. J. Biochem., Tokyo 103, 386–392 (1988).
Schwyter, D., Phillips, M. & Reisler, E. Biochemistry 28, 5889–5895 (1989).
Carlsson, L. et al. J. molec. Biol. 105, 353–366 (1976).
Schutt, C. E., Lindberg, U., Myslik, J. & Strauss, N. J. molec. Biol. 209, 735–746 (1989).
Vandekerckhove, J. S., Kaiser, D. A. & Pollard, T. D. J. Cell Biol. 109, 619–626 (1989).
Kuwayama, H. & Yount, R. G. Biophys. J. 49, 454a (1986).
Hegyi, Szilagyi, L. & Elzinga, M. Biochemistry 25, 5793–5798 (1986).
Saenger, W. Principles of Nucleic Acid Structure 74 (Springer-Verlag, 1984).
DePhamphilis, M. L. & Cleland, W. W. Biochemistry 12, 3714–3723 (1973).
Strzelecka-Golaszewska, H., Boguta, G., Zmorzynski, S. & Moraczewska, J. Eur. J. Biochem. 182, 299–305 (1989).
Nowak, E., Strzelecka-Golaszewska, H. & Goody, R. S. Biochemistry 27, 1785–1792 (1988).
Loscalzo, J. & Reed, G. H. Biochemistry, 15, 5407–5412 (1976).
Brauer, M. & Sykes, B. D. Biochemistry 21, 5934–5939 (1982).
Miki, M. & Wahl, P. Biochim. biophys. Acta 828, 188–195 (1985).
Valentin-Ranc, C. & Carlier, M.-F. J. biol. Chem. 264, 20871–20880 (1989).
Moore, P. B., Huxley, H. E. & DeRosier, D. J. J. molec. Biol. 50, 279–295 (1970).
Sutoh, K. Biochemistry 21, 3654–3661 (1982).
Bertrand, R. et al. Biochemistry 27, 5728–5736 (1988).
Méjean, C. et al. Biosci. Rept 6, 493–499 (1986).
Miller, L., Kalnowski, M., Yunossi, Z., Bulsinki, J. C. & Reisler, E. Biochemistry 26, 6064–6070 (1987).
Moir, A. J. G., Levine, B. A., Goodearl, A. J. & Trayer, I. P. J. Muscle Res. Cell Motil. 8, 68–69 (1988).
Barden, J. A., Phillips, L., Cornell, B. A. & dos Remedios, C. G. Biochemistry 28, 5895–5901 (1989).
Barden, J. A. & Phillips, L. Biochemistry 29, 1348–1354 (1990).
Szilagyi, L. & Lu, R. C. Biochim. Biophys. Acta 709, 204–211 (1982).
Trayer, I. P., Trayer, H. R. & Levine, B. A. Eur. J. Biochem. 164, 259–266 (1987).
Flaherty, K. M., DeLuca-Flaherty, C. & McKay, D. B. Nature 346, 623–628 (1990).
Blum, M., Metcalf, P. & Wiley, D. C. J. appl. Crystallogr. 20, 235–247 (1987).
dos Remedios, C., Miki, M. & Barden, J. A. J. Muscle Res. Cell Motil. 8, 97–117 (1987).
Priestle, J. P. J. appl. Crystallogr. 21, 572–576 (1988).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Kabsch, W., Mannherz, H., Suck, D. et al. Atomic structure of the actin: DNase I complex . Nature 347, 37–44 (1990). https://doi.org/10.1038/347037a0
Issue Date:
DOI: https://doi.org/10.1038/347037a0
This article is cited by
-
Bound nucleotide can control the dynamic architecture of monomeric actin
Nature Structural & Molecular Biology (2022)
-
Human deafness-associated variants alter the dynamics of key molecules in hair cell stereocilia F-actin cores
Human Genetics (2022)
-
Cyclophosphamide treatment evoked side effect on skeletal muscle actin, monitored by DSC
Journal of Thermal Analysis and Calorimetry (2022)
-
Dose-dependent effect of cyclophosphamide treatment on actin
Journal of Thermal Analysis and Calorimetry (2022)
-
Alterations of inter-domain flexibility in actin monomers during cyclophosphamide treatment
Journal of Thermal Analysis and Calorimetry (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.