Structural Polymorphism of Actin

Toshiro Oda, Shuichi Takeda, Akihiro Narita, Yuichiro Maéda

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

Abstract

Information on the structural polymorphism of a protein is essential to understand the mechanisms of how it functions at an atomic level. Numerous studies on actin have accumulated substantial amounts of information about its polymorphism, and there are over 200 published atomic structures of different forms of actin using crystallography, fiber diffraction, and electron microscopy. To characterize all the reported structures, we proposed simple parameters based on the discrete rigid bodies within the actin molecule and identified four conformation groups by cluster analysis: the F-form in naked F-actin, the C-form in cofilactin, the O-form in profilin–actin, and the G-form in the majority of actin-containing crystal structures. The G-form group included the most variations, but each conformational variation was convertible via a thermal fluctuation, whereas the F- and C-forms were not accessible from the G-form. The convertibility and accessibility of the structures were evaluated using molecular dynamics simulations. Information about conformational conversion among each group is useful for understanding the mechanisms of actin function.

Original languageEnglish
Pages (from-to)3217-3228
Number of pages12
JournalJournal of Molecular Biology
Volume431
Issue number17
DOIs
Publication statusPublished - Aug 9 2019
Externally publishedYes

Keywords

  • clustering
  • conformational space
  • domain orientation
  • protein assembly
  • rigid bodies

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Molecular Biology

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