Metal binding to the dynamic cytoplasmic domain of the cation diffusion facilitator (CDF) protein MamM induces a 'locked-in' configuration

Barber-Zucker, Shiran, Hall, Jenny, Mangapuram, Sivasubramanyan Venkata, Kass, Itamar, Kolusheva, Sofiya, MacMillan, Fraser, Zarivach, Raz and Henn, Arnon (2019) Metal binding to the dynamic cytoplasmic domain of the cation diffusion facilitator (CDF) protein MamM induces a 'locked-in' configuration. FEBS Journal, 286 (11). pp. 2193-2215. ISSN 1742-464X

[img]
Preview
PDF (Accepted_Manuscript) - Submitted Version
Download (2MB) | Preview

Abstract

Cation diffusion facilitator (CDF) proteins are a conserved family of transmembrane transporters that ensure cellular homeostasis of divalent transition metal cations. Metal cations bind to CDF protein's cytoplasmic C-terminal domain (CTD), leading to closure from its apo open V-shaped dimer to a tighter packed structure, followed by a conformational change of the transmembrane domain thus enabling transport of the metal cation. By implementing a comprehensive range of biochemical and biophysical methods, we studied the molecular mechanism of metal binding to the magnetotactic bacterial CDF protein MamM CTD. Our results reveal that the CTD is rather dynamic in its apo form, and that two dependent metal binding sites, a single central binding site and two symmetrical, peripheral sites, are available for metal binding. However, only cation binding to the peripheral sites leads to conformational changes that lock the protein in a compact state. Thus, this work reveals how metal binding is regulating the sequential uptakes of metal cations by MamM, and extends our understanding of the complex regulation mechanism of CDF proteins. This article is protected by copyright. All rights reserved.

Item Type: Article
Additional Information: This article is protected by copyright. All rights reserved.
Faculty \ School: Faculty of Science > School of Chemistry
Depositing User: LivePure Connector
Date Deposited: 04 Mar 2019 16:30
Last Modified: 09 Oct 2020 23:53
URI: https://ueaeprints.uea.ac.uk/id/eprint/70094
DOI: 10.1111/febs.14795

Actions (login required)

View Item View Item