6yir
From Proteopedia
Crystal structure of Bacillus subtilis MsmX ATPase
Structural highlights
FunctionMSMX_BACSU Part of the ABC transporter complex involved in maltodextrin import (Probable). Is also part of the ABC transporter complex MelEDC-MsmX involved in melibiose, raffinose and stachyose import (PubMed:31138628). Probably responsible for energy coupling to the transport system (Probable).[1] [2] Publication Abstract from PubMedATP-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. Multitask ATPases (NBDs) of bacterial ABC importers type I and their interspecies exchangeability.,Leisico F, Godinho LM, Goncalves IC, Silva SP, Carneiro B, Romao MJ, Santos-Silva T, de Sa-Nogueira I Sci Rep. 2020 Nov 11;10(1):19564. doi: 10.1038/s41598-020-76444-0. PMID:33177617[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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