N. Zeytuni

TL;DR: This review considers the structural features of TPR domains that permit the great ligand-binding diversity of this motif, given that TPR-interacting partners display variations in both sequence and secondary structure.

TL;DR: It is proposed that MamA self-assembles through its putative TPR motif and its concave site to create a large homooligomeric scaffold which can interact with other magnetosome-associated proteins via the MamA convex site.

TL;DR: This work employed a multi-disciplinary approach to study the activation mechanism of the CDF protein family using MamM, one of the main ion transporters of magnetosomes – bacterial organelles that enable magnetotactic bacteria to orientate along geomagnetic fields.

TL;DR: The results suggest that the magnetosome membrane is specifically associated with a small subset of integral proteins that are tightly packed within the lipid layer that will help to elucidate the complex process of magnetosomes biogenesis.

TL;DR: It is shown that MamB is most likely an active magnetosome‐directed transporter serving two distinct, yet essential functions: first, MamB initiates magnetosomes vesicle formation in a transport‐independent process, probably by serving as a landmark protein, and second, Mam B transport activity is required for magnetite nucleation.