Multitask ATPases (NBDs) of bacterial ABC importers type I and their interspecies exchangeability
- Citation:
- Leisico, F, Godinho LM, Gonçalves IC, Silva SP, Carneiro B, Romão MJ, Santos-Silva T, de Sá-Nogueira I. 2020. Multitask ATPases (NBDs) of bacterial ABC importers type I and their interspecies exchangeability, 2020. 10(1):19564.
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 interspecies ABC type I importers in which the NBDs could be exchanged. Furthermore, the first crystal structure of an assigned multitask NBD provides a framework to understand the molecular basis of the broader specificity of interaction with the TMDs.
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