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Three-dimensional structure of acanthamoeba castellanii myosin-ib (mib) determined by cryoelectron microscopy of decorated actin filaments

Academic Article
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Overview

related to degree

  • Jontes, James David, Ph.D. in Biology, Scripps Research 1992 - 1997

authors

  • Jontes, James David
  • Ostap, E. M.
  • Pollard, T. D.
  • Milligan, Ronald

publication date

  • April 1998

journal

  • Journal of Cell Biology  Journal

abstract

  • The Acanthamoeba castellanii myosin-Is were the first unconventional myosins to be discovered, and the myosin-I class has since been found to be one of the more diverse and abundant classes of the myosin superfamily. We used two-dimensional (2D) crystallization on phospholipid monolayers and negative stain electron microscopy to calculate a projection map of a "classical" myosin-I, Acanthamoeba myosin-IB (MIB), at approximately 18 A resolution. Interpretation of the projection map suggests that the MIB molecules sit upright on the membrane. We also used cryoelectron microscopy and helical image analysis to determine the three-dimensional structure of actin filaments decorated with unphosphorylated (inactive) MIB. The catalytic domain is similar to that of other myosins, whereas the large carboxy-terminal tail domain differs greatly from brush border myosin-I (BBM-I), another member of the myosin-I class. These differences may be relevant to the distinct cellular functions of these two types of myosin-I. The catalytic domain of MIB also attaches to F-actin at a significantly different angle, approximately 10 degrees, than BBM-I. Finally, there is evidence that the tails of adjacent MIB molecules interact in both the 2D crystal and in the decorated actin filaments.

subject areas

  • Acanthamoeba
  • Actins
  • Animals
  • Crystallization
  • Freezing
  • Microscopy, Electron
  • Microvilli
  • Models, Molecular
  • Myosins
  • Phospholipids
  • Protein Conformation
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Identity

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.141.1.155

PubMed ID

  • 9531555
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Additional Document Info

start page

  • 155

end page

  • 162

volume

  • 141

issue

  • 1

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