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Biochemists reveal how complex molecule moves iron through body OhioState NatureComms
, we propose that the overall negatively charged cluster weakly associates through electrostatic complementation with the linking helical stretches between the TM-domains and the NBDs, which expose positively charged residues .
Next, the cargo is recruited to conserved motifs of the binding pocket, coupled to initiation of occlusion and perhaps nucleotide binding, as observed in the partially occluded CtAtm1structure. Our data are inconclusive regarding the nature of the bound cargo because only parts of the cluster are detected, although flexibility may partly explain this observation.
Subsequently, full occlusion is achieved, a conformation in which the cargo is inaccessible for the surrounding environment . In this structure, CtAtm1, we were unable to detect internalized cargo, as has also been the case for all occluded structures Atm1 proteins. However, a considerable pocket remains, although the part of it that is in direct contact with the inner gate has been divided into two portions .
Eventually, cargo release occurs, associated with outward-facing configurations. Displacement of the cargo from the pocket is likely stimulated by reorganization of the inner gate, as detected from the CtAtm1
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