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Mode of Interaction of the Signal-Transducing Protein EIIAGlc with the Maltose ABC Transporter in the Process of Inducer Exclusion

Published inBiochemistry, vol. 55, no. 38, p. 5442-5452
Publication date2016-09-19
First online date2016-09-19
Abstract

Enzyme IIAGlc (EIIAGlc) of the phosphoenolpyruvate phosphotransferase system for the uptake of glucose in Escherichia coli and Salmonella inhibits the maltose ATP-binding cassette transporter (MalE-FGK2) by interaction with the nucleotide-binding and -hydrolyzing subunit MalK, a process termed inducer exclusion. We have investigated binding of EIIAGlc to the MalK dimer by cysteine cross-linking in proteoliposomes. The results prove that the binding site I of EIIAGlc is contacting the N-terminal subdomain of MalK while the binding site II is relatively close to the C-terminal (regulatory) subdomain, in agreement with a crystal structure [Chen, S., Oldham, M. L., Davidson, A. L., and Chen, J. (2013) Nature499, 364−368]. Moreover, EIIAGlc was found to bind to the MalK dimer regardless of its conformational state. Deletion of the amphipathic N-terminal peptide of EIIAGlc, which is required for inhibition, reduced formation of cross-linked products. Using a spin-labeled transporter variant and EPR spectroscopy, we demonstrate that EIIAGlc arrests the transport cycle by inhibiting the ATP-dependent closure of the MalK dimer.

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Citation (ISO format)
WUTTGE, Steven et al. Mode of Interaction of the Signal-Transducing Protein EIIA<sup>Glc</sup> with the Maltose ABC Transporter in the Process of Inducer Exclusion. In: Biochemistry, 2016, vol. 55, n° 38, p. 5442–5452. doi: 10.1021/acs.biochem.6b00721
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ISSN of the journal0006-2960
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