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

DOI: 10.1016/j.bbrc.2019.08.013

Authors: Michela Bollati (Consiglio Nazionale delle Ricerche; Università degli Studi di Milano) , Emanuele Scalone (Consiglio Nazionale delle Ricerche; Università degli Studi di Milano) , Francesco Boni (Consiglio Nazionale delle Ricerche; Università degli Studi di Milano) , Eloise Mastrangelo (Consiglio Nazionale delle Ricerche; Università degli Studi di Milano) , Toni Giorgino (Consiglio Nazionale delle Ricerche; Università degli Studi di Milano) , Mario Milani (Consiglio Nazionale delle Ricerche; Università degli Studi di Milano) , Matteo De Rosa (Consiglio Nazionale delle Ricerche; Università degli Studi di Milano)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Biochemical And Biophysical Research Communications

State: Published (Approved)
Published: August 2019
Diamond Proposal Number(s): 20221

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.

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

Diamond Keywords: Amyloidosis

Subject Areas: Biology and Bio-materials


Instruments: I04-Macromolecular Crystallography

Added On: 15/08/2019 09:27

Discipline Tags:

Non-Communicable Diseases Health & Wellbeing Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)