The metal binding site composition of the cation diffusion facilitator protein MamM cytoplasmic domain impacts its metal responsivity.

ABSTRACT: The cation diffusion facilitator (CDF) is a conserved family of divalent d-block metal cation transporters that extrude these cations selectively from the cytoplasm. CDF proteins are composed of two domains: the transmembrane domain, through which the cations are transported, and a regulatory cytoplasmic C-terminal domain (CTD). It was recently shown that the CTD of the CDF protein MamM from magnetotactic bacteria has a role in metal selectivity, as binding of different metal cations exhibits distinctive affinities and conformations. It is yet unclear whether the composition of the CTD binding sites can impact metal selectivity and if we can manipulate the CTD to response to other non-native metals in CDF proteins. Here we performed a mutational study of the model protein MamM CTD, where w

SUBMITTER: Barber-Zucker S 

PROVIDER: S-EPMC7441159 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature