Multitask ATPases (NBDs) of bacterial ABC importers type I and their interspecies exchangeability.

ABSTRACT: ATP-binding cassette (ABC) type I importers are widespread in bacteria and play a crucial role in its survival and pathogenesis. They share the same modular architecture comprising two intracellular nucleotide-binding domains (NBDs), two transmembrane domains (TMDs) and a substrate-binding protein. The NBDs bind and hydrolyze ATP, thereby generating conformational changes that are coupled to the TMDs and lead to substrate translocation. A group of multitask NBDs that are able to serve as the cellular motor for multiple sugar importers was recently discovered. To understand why some ABC importers share energy-coupling components, we used the MsmX ATPase from Bacillus subtilis as a model for biological and structural studies. Here we report the first examples of functional hybrid interspecie

SUBMITTER: Leisico F 

PROVIDER: S-EPMC7658222 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature