@article {16658,
	title = {Multitask ATPases (NBDs) of bacterial ABC importers type I and their interspecies exchangeability},
	volume = {10},
	year = {2020},
	note = {n/a},
	month = {2020},
	pages = {19564},
	abstract = {<p>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.</p>
},
	isbn = {2045-2322},
	url = {https://doi.org/10.1038/s41598-020-76444-0},
	author = {Leisico, Francisco and Lia M. Godinho and Gon{\c c}alves, In{\^e}s C. and Silva, Sara P. and Carneiro, Bruno and Rom{\~a}o, Maria J. and Santos-Silva, Teresa and Isabel de S{\'a}-Nogueira}
}
