Two molybdate/tungstate ABC transporters that interact very differently with their substrate binding proteins.

ABSTRACT: In all kingdoms of life, ATP Binding Cassette (ABC) transporters participate in many physiological and pathological processes. Despite the diversity of their functions, they have been considered to operate by a largely conserved mechanism. One deviant is the vitamin B12 transporter BtuCD that has been shown to operate by a distinct mechanism. However, it is unknown if this deviation is an exotic example, perhaps arising from the nature of the transported moiety. Here we compared two ABC importers of identical substrate specificity (molybdate/tungstate), and find that their interactions with their substrate binding proteins are utterly different. One system forms a high-affinity, slow-dissociating complex that is destabilized by nucleotide and substrate binding. The other forms a low-affini

SUBMITTER: Vigonsky E 

PROVIDER: S-EPMC3619290 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature