Abstract
The magnesium channel MgtE is the primary magnesium transport system in ∼50% of bacteria, and its eukaryotic homologs are SLC41 family of solute carriers. The full-length MgtE from T. thermophilus is a homodimeric Mg2+ channel, which contains transmembrane and cytosolic domains. The cytoplasmic domain is divided into two sub-domains, namely the super-helical N-domain and cystathione-β-synthase (CBS) domain. The N-domain, in particular, is proposed to primarily function as a Mg2+ sensor. Here, we have monitored the folding and structural stability of the isolated cytoplasmic domain of MgtE (MgtETT-CD) in the presence of protein denaturing conditions.
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