Further insights into the metal ion binding abilities and the metalation pathway of a plant metallothionein from Musa acuminata.

ABSTRACT: The superfamily of metallothioneins (MTs) combines a diverse group of metalloproteins, sharing the characteristics of rather low molecular weight and high cysteine content. The latter provides MTs with the capability to coordinate thiophilic metal ions, in particular those with a d ¹⁰ electron configuration. The sub-family of plant MT3 proteins is only poorly characterized and there is a complete lack of three-dimensional structure information. Building upon our previous results on the Musa acuminata MT3 (musMT3) protein, the focus of the present work is to understand the metal cluster formation process, the role of the single histidine residue present in musMT3, and the metal ion binding affinity. We concentrate our efforts on the coordination of Zn^II and Cd^II</

SUBMITTER: Cabral ACS 

PROVIDER: S-EPMC5756683 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature