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• W1978482772 abstract "The X-ray crystal structure of a member of the glucose-specific phosphotransferase system (EIIAGlc) bound to the MalFGK2 maltose transporter is presented, revealing that two EIIAGlcproteins bind to the cytoplasmic ATPase subunits of the maltose transporter to stabilize it in an inward-facing conformation that prevents ATP hydrolysis. When a preferred carbon source is available, bacteria use a system known as carbon catabolite repression (CCR) to halt the synthesis and activity of proteins involved in the usage of less-preferred carbon sources. In Escherichia coli the glucose-specific phosphotransferase system, enzyme IIA (EIIAGlc), is central to this control system, and when glucose is available in the environment transport of other sugars, such as maltose, is shut down. This paper reports the X-ray crystal structure of a EIIAGlc bound to the MalFGK2 maltose transporter. The structure reveals that two EIIAGlc molecules bind to the cytoplasmic ATPase subunits of the maltose transporter, stabilizing it in an inward-facing conformation and preventing the structural rearrangements necessary for ATP hydrolysis — and maltose transport. Efficient carbon utilization is critical to the survival of microorganisms in competitive environments. To optimize energy usage, bacteria have developed an integrated control system to preferentially uptake carbohydrates that support rapid growth. The availability of a preferred carbon source, such as glucose, represses the synthesis and activities of proteins necessary for the transport and metabolism of secondary carbon sources. This regulatory phenomenon is defined as carbon catabolite repression1. In enteric bacteria, the key player of carbon catabolite repression is a component of the glucose-specific phosphotransferase system, enzyme IIA (EIIAGlc)1,2. It is known that unphosphorylated EIIAGlc binds to and inhibits a variety of transporters when glucose is available1,2. However, understanding the underlying molecular mechanism has been hindered by the complete absence of structures for any EIIAGlc–transporter complexes. Here we present the 3.9 Å crystal structure of Escherichia coli EIIAGlc in complex with the maltose transporter, an ATP-binding cassette (ABC) transporter. The structure shows that two EIIAGlc molecules bind to the cytoplasmic ATPase subunits, stabilizing the transporter in an inward-facing conformation and preventing the structural rearrangements necessary for ATP hydrolysis. We also show that the half-maximal inhibitory concentrations of the full-length EIIAGlc and an amino-terminal truncation mutant differ by 60-fold, consistent with the hypothesis that the amino-terminal region, disordered in the crystal structure, functions as a membrane anchor to increase the effective EIIAGlc concentration at the membrane3,4. Together these data suggest a model of how the central regulatory protein EIIAGlc allosterically inhibits maltose uptake in E. coli." @default.
• W1978482772 created "2016-06-24" @default.
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• W1978482772 date "2013-06-16" @default.
• W1978482772 modified "2023-10-14" @default.
• W1978482772 title "Carbon catabolite repression of the maltose transporter revealed by X-ray crystallography" @default.
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• W1978482772 doi "https://doi.org/10.1038/nature12232" @default.
• W1978482772 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3875231" @default.
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