High-resolution crystal structure of gelsolin domain 2 in complex with the physiological calcium ion

Biochem Biophys Res Commun. 2019 Oct 8;518(1):94-99. doi: 10.1016/j.bbrc.2019.08.013. Epub 2019 Aug 12.

Abstract

The second domain of gelsolin (G2) hosts mutations responsible for a hereditary form of amyloidosis. The active form of gelsolin is Ca2+-bound; it is also a dynamic protein, hence structural biologists often rely on the study of the isolated G2. However, the wild type G2 structure that have been used so far in comparative studies is bound to a crystallographic Cd2+, in lieu of the physiological calcium. Here, we report the wild type structure of G2 in complex with Ca2+ highlighting subtle ion-dependent differences. Previous findings on different G2 mutations are also briefly revised in light of these results.

Keywords: AGel amyloidosis; Calcium; Gelsolin; Pathogenic mutations; X-ray crystallography.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Calcium / metabolism*
  • Crystallography, X-Ray
  • Gelsolin / chemistry*
  • Gelsolin / metabolism*
  • Ions
  • Models, Molecular
  • Mutant Proteins / chemistry
  • Mutant Proteins / metabolism
  • Mutation / genetics
  • Protein Binding
  • Protein Domains

Substances

  • Gelsolin
  • Ions
  • Mutant Proteins
  • Calcium