Literature summary for 7.5.2.6 extracted from

Weng, J.; Fan, K.; Wang, W.
The conformational transition pathway of ATP binding cassette transporter MsbA revealed by atomistic simulations (2010), J. Biol. Chem., 285, 3053-3063.

Crystallization (Commentary)

Crystallization (Comment)	Organism
targeted molecular dynamics simulation methods reveal a clear spatiotemporal order of the conformational movements from the outward-facing to the inward-facing states. The disruption of the nucleotide binding sites at the nucleotide-binding dimer interface is the very first event that initiates the following conformational changes. The conserved x-loops of the nucleotide binding sites participate in the interaction network that stabilizes the cytoplasmic tetrahelix bundle of the transmembrane domains and play an important role in mediating the cross-talk between the nucleotide-binding domains and transmembrane domains. The movement of the nucleotide-binding domain dimer is transmitted through x-loops to break the tetrahelix bundle, inducing the packing rearrangements of the transmembrane helices at the cytoplasmic side and the periplasmic side sequentially	Escherichia coli

Crystallization (Comment)

Organism

targeted molecular dynamics simulation methods reveal a clear spatiotemporal order of the conformational movements from the outward-facing to the inward-facing states. The disruption of the nucleotide binding sites at the nucleotide-binding dimer interface is the very first event that initiates the following conformational changes. The conserved x-loops of the nucleotide binding sites participate in the interaction network that stabilizes the cytoplasmic tetrahelix bundle of the transmembrane domains and play an important role in mediating the cross-talk between the nucleotide-binding domains and transmembrane domains. The movement of the nucleotide-binding domain dimer is transmitted through x-loops to break the tetrahelix bundle, inducing the packing rearrangements of the transmembrane helices at the cytoplasmic side and the periplasmic side sequentially

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

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Release 2023.1 (January 2023)