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a periplasmic maltose-binding protein, MBP, is required to stimulate the ATPase activity of the transporter. MBP stimulates ATP hydrolysis and initiates the transport process, it must interact with the resting state conformation to form a pretranslocation complex that is metastable in order to advance to the outward-facing conformation in the presence of ATP
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about 10dolf stimulation of activity at 0.005 mM
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required by wild-type strain, mutant strain does not require maltose-binding protein for transport. The major function of the maltose-binding protein is to send a transmembrane signal, in the presence of ligands, to the ATPase subunits on the inner side of the membrane. In addition it performs a special function in the translocation of the larger ligands, maltodextrins, perhaps by aligning them from entry into the channel
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stimulates detergent-soluble maltose transporter, does not change the affinity of the complex for ATP but does increase the maximal rate of ATP hydrolysis
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Characterization of the structural requirements for assembly and nucleotide binding cassette transporter. The maltose transport system of Escherichia coli
1993
Panagiotidis, C.H.; Reyes, M.; Sievertsen, A.; Boos, W.; Shuman, H.A.
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Maltose transport system of Escherichia coli: an ABC-type transporter
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Nikaido, H.
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The detergent-soluble maltose transporter is activated by maltose binding protein and verapamil
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Reich-Slotky, R.; Panagiotidis, C.; Reyes, M.; Shuman, H.A.
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Comparison of varicella-zoster virus ORF47 protein kinase and casein kinase II and their substrates
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J. Med. Virol.
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Crystal structure of the maltose transporter in a pretranslocation intermediate state
2011
Oldham, M.; Chen, J.
Science
332
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Full engagement of liganded maltose-binding protein stabilizes a semi-open ATP-binding cassette dimer in the maltose transporter
2015
Alvarez, F.J.; Orelle, C.; Huang, Y.; Bajaj, R.; Everly, R.M.; Klug, C.S.; Davidson, A.L.
Mol. Microbiol.
98
878-894
Structural and functional characterization of a maltose/maltodextrin ABC transporter comprising a single solute binding domain (MalE) fused to the transmembrane subunit MalF
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Licht, A.; Bommer, M.; Werther, T.; Neumann, K.; Hobe, C.; Schneider, E.
Res. Microbiol.
170
1-12