Abstract
A single high-resolution model for the F-actin filament has been generated by refining the structure of a crystallographically determined skeletal muscle G-actin subunit against X-ray fiber diffraction data (Holmes et al. 1990; Lorenz et al. 1993). However, electron microscopic studies have shown at low-resolution that the actin filament can exist in multiple conformations as a function of the bound metal (Orlova and Egelman 1995), the nucleotide (Orlova and Egelman 1993), the isoform of actin involved (Orlova et al. 1997), and the presence of other proteins bound to actin (Owen and DeRosier 1993; McGough et al. 1997). It is thus informative to ask what is known about different structural states of G-actin.
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References
Belmont LD, Drubin DG (1998) The yeast v159n actin mutant reveals roles for actin dynamics in vivo. J Cell Biol 142: 1289–1299
Belmont LD, Orlova A, Drubin DG, Egelman EH (1999) A change in actin conformation associated with filament instability after Pi release. ProcNatAcadSci, USA 96: 29–34
Chik JK, Lindberg U, Schutt CE (1996) The structure of an open state of beta-actin at 265 A resolution. J Mol Biol 263: 607–623
Egelman EH, Orlova A (1995) New insights into actin filament dynamics. Cur Opin Struct Biol 5: 172–180
Egelman EH, Yu X (1989) The location of DNA in RecA-DNA helical filaments. Science 245: 404–407
Holmes KC, Popp D, Gebhard W, Kabsch W (1990) Atomic model of the actin filament. Nature 347: 44–49
Kabsch W, Mannherz HG, Suck D, Pai EF, Holmes KC (1990) Atomic structure of the actin: DNase I complex. Nature 347: 37–44
Kraulis PJ (1991) MOLSCRIPT: A program to produce both detailed schematic plots of protein structures. J Appl Crystallogr 24: 946–950
Lorenz M, Popp D, Holmes KC (1993) Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. J Mol Biol 234: 826–836
McGough A, Pope B, Chiu W, Weeds A (1997) Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function. J Cell Biol 138: 771–781
McLaughlin PJ, Gooch JT, Mannherz HG, Weeds AG (1993) Structure of gelsolin segment 1-actin complex and the mechanism of filament severing. Nature 364: 685–692
Orlova A, Egelman EH (1993) A conformational change in the actin subunit can change the flexibility of the actin filament. J Mol Biol 232: 334–341
Orlova A, Egelman EH (1995) Structural dynamics of F-actin I Changes in the C-terminus. J Mol Biol 245: 582–597
Orlova A, Chen X, Rubenstein PA, Egelman EH (1997) Modulation of yeast F-actin structure by a mutation in the nucleotide-binding cleft. J Mol Biol 271: 235–243
Owen C, DeRosier D (1993) A 13 A map of the actin-scruin filament from the Limulus acrosomal process. J Cell Biol 123: 337–344
Schutt CE, Myslik JC, Rozycki MD, Goonesekere NCW, Lindberg U (1993) The structure of crystalline profilin β-actin. Nature 365: 810–816
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© 2001 Springer-Verlag Berlin Heidelberg
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Egelman, E.H., Orlova, A. (2001). Two Conformations of G-Actin Related to Two Conformations of F-Actin. In: dos Remedios, C.G., Thomas, D.D. (eds) Molecular Interactions of Actin. Results and Problems in Cell Differentiation, vol 32. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-46560-7_7
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DOI: https://doi.org/10.1007/978-3-540-46560-7_7
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