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Volume 272, Number 7, Issue of February 14, 1997 pp. 4261-4268
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Three-dimensional Structure of Myelin Basic Protein
I. RECONSTRUCTION VIA ANGULAR RECONSTITUTION OF RANDOMLY ORIENTED SINGLE PARTICLES

(Received for publication, September 19, 1996)

Daniel R. Beniac , Maria D. Luckevich , Gregory J. Czarnota ^§ , Thomas A. Tompkins ^¶ , Ross A. Ridsdale , F. Peter Ottensmeyer ^§ , Mario A. Moscarello ^¶ and George Harauz

From the  Department of Molecular Biology and Genetics, University of Guelph, Guelph, Ontario N1G 2W1, Canada, ^§ Department of Molecular and Structural Biology, Ontario Cancer Institute, 610 University Avenue, Toronto, Ontario M5G 2M9, Canada, and ^¶ Department of Biochemistry Research, Hospital for Sick Children, 555 University Avenue, Toronto, Ontario M5G 1X8, Canada

Myelin basic protein (MBP) plays an integral role in the structure and function of the myelin sheath. In humans and cattle, an 18.5-kDa isoform of MBP predominates and exists as a multitude of charge isomers resulting from extensive and varied post-translational modifications. We have purified the least modified isomer (named C1) of the 18.5-kDa isoform of MBP from fresh bovine brain and imaged this protein as negatively stained single particles adsorbed to a lipid monolayer. Under these conditions, MBP/C1 presented diverse projections whose relative orientations were determined using an iterative quaternion-assisted angular reconstitution scheme. In different buffers, one with a low salt and the other with a high salt concentration, the conformation of the protein was slightly different. In low salt buffer, the three-dimensional reconstruction, solved to a resolution of 4 nm, had an overall "C" shape of outer radius 5.5 nm, inner radius 3 nm, overall circumference 15 nm, and height 4.7 nm. The three-dimensional reconstruction of the protein in high salt buffer, solved to a resolution of 2.8 nm, was essentially the same in terms of overall dimensions but had a somewhat more compact architecture. These results are the first structures achieved directly for this unusual macromolecule, which plays a key role in the development of multiple sclerosis.

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