6YIR

Crystal structure of Bacillus subtilis MsmX ATPase

Summary for 6YIR

• Entry DOI: 10.2210/pdb6yir/pdb
• Descriptor: Oligosaccharides import ATP-binding protein MsmX, SULFATE ION, TRIETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: atpase, polysaccharide import, multitask, hydrolase
• Biological source: Bacillus subtilis (strain 168)
• Total number of polymer chains: 1
• Total formula weight: 42686.22

Authors

Leisico, F.,Santos-Silva, T.,Romao, M.J. (deposition date: 2020-04-01, release date: 2020-11-18, Last modification date: 2024-01-24)

Primary citation

Leisico, F.,Godinho, L.M.,Goncalves, I.C.,Silva, S.P.,Carneiro, B.,Romao, M.J.,Santos-Silva, T.,de Sa-Nogueira, I.
Multitask ATPases (NBDs) of bacterial ABC importers type I and their interspecies exchangeability.
Sci Rep, 10:19564-19564, 2020

PubMed 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.

PubMed: 33177617
DOI: 10.1038/s41598-020-76444-0

Experimental method

X-RAY DIFFRACTION (1.68 Å)