Activation in isolation: Exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin

Kartik Narayan, Sakesit Chumnarnsilpa, Han Choe, Edward Irobi, Dunja Urosev, Uno Lindberg, Clarence E. Schutt, Leslie D. Burtnick, Robert C. Robinson

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

Gelsolin requires activation to carry out its severing and capping activities on F-actin. Here, we present the structure of the isolated C-terminal half of gelsolin (G4-G6) at 2.0 Å resolution in the presence of Ca2+ ions. This structure completes a triptych of the states of activation of G4-G6 that illuminates its role in the function of gelsolin. Activated G4-G6 displays an open conformation, with the actin-binding site on G4 fully exposed and all three type-2 Ca2+ sites occupied. Neither actin nor the type-l Ca2+, which normally is sandwiched between actin and G4, is required to achieve this conformation.

Original languageEnglish
Pages (from-to)82-85
Number of pages4
JournalFEBS Letters
Volume552
Issue number2-3
DOIs
Publication statusPublished - Sep 25 2003
Externally publishedYes

Keywords

  • Actin
  • Calcium-activation
  • Gelsolin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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    Narayan, K., Chumnarnsilpa, S., Choe, H., Irobi, E., Urosev, D., Lindberg, U., Schutt, C. E., Burtnick, L. D., & Robinson, R. C. (2003). Activation in isolation: Exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin. FEBS Letters, 552(2-3), 82-85. https://doi.org/10.1016/S0014-5793(03)00933-5