Hostname: page-component-848d4c4894-x24gv Total loading time: 0 Render date: 2024-05-27T01:42:46.291Z Has data issue: false hasContentIssue false
  • English
  • Français

3D Reconstruction of Smooth Muscle A-Actinin by Cryo Electron Microscopy

Published online by Cambridge University Press:  02 July 2020

Jun Liu ,
Dianne Taylor  and
Kenneth A. Taylor
Jun Liu
Affiliation:
Institute of Molecular Biophysics, Florida State University, Tallahassee, FL32306
Dianne Taylor
Affiliation:
Institute of Molecular Biophysics, Florida State University, Tallahassee, FL32306
Kenneth A. Taylor
Affiliation:
Institute of Molecular Biophysics, Florida State University, Tallahassee, FL32306
Get access

Extract

α-Actinin is an actin crosslinking protein identified in a wide variety of cells. Both muscle and nonmuscle isoforms of α-actinin have been characterized [1]. The molecule consists of two polypeptide chains that form a rod-shaped antiparallel dimer. Each polypeptide is composed of three distinct structural regions: actin-binding domain, four triple helical repeats that form a central rod, and a carboxyl terminal domain that contains two EF hand calcium-binding sites. Here we present the 3D structure of the smooth muscle α-actinin, as determined by cryo electron microscopy at 2.0 nm resolution.

Two dimensional crystals of chicken gizzard α-actinin were formed on positively charged lipid monolayer [2] and preserved frozen hydrated for TEM. The crystal has a unit cell dimension of a = 26.31 nm, b = 20.37 nm, γ= 107.10°, based on internal calibration against TMV.

Type
Electron Cryomicroscopy of Macromolecules
Information
Microscopy and Microanalysis , Volume 6 , Issue S2: Proceedings: Microscopy & Microanalysis 2000, Microscopy Society of America 58th Annual Meeting, Microbeam Analysis Society 34th Annual Meeting, Microscopical Society of Canada/Societe de Microscopie de Canada 27th Annual Meeting, Philadelphia, Pennsylvania August 13-17, 2000 , August 2000 , pp. 244 - 245
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]Blanchard, A., Ohanian, V. and Critchley, D., J. Muscle Res. Cell Motil. (1989) 10, 280.CrossRefGoogle Scholar
[2]Taylor, K.A. and Taylor, D., J. Mol. Biol. (1993) 230, 196.CrossRefGoogle Scholar
[3]Schmid, M.R. and Tarn, M., Ultramicroscopy (1993) 48, 251.CrossRefGoogle Scholar
[4]Goldsmith, S.C., Pokala, N., Shen, W., Federov, A.A., Matsudaira, P., Almo, S.C., Nat. Struct. Biol. (1997) 4, 708.CrossRefGoogle Scholar
[5]Zhang, M., Tanaka, T. and Ikura, M., Nat. Struct. Biol. (1995) 2, 758.CrossRefGoogle Scholar
[6]Djinovic-Carugo, K., Young, P., Gautel, M. and Saraste, M., Cell (1999) 98, 537.CrossRefGoogle Scholar
[7]Jones, T.A., Zou, J.Y., Cowan, S.W. and Kjeldgaard, M., Acta Cryst. (1991) A47, 110.CrossRefGoogle Scholar