Abstract
The lactose repressor protein from Escherichia coli binds sugars, primarily galactosides, which modulate its interactions with operator DNA and thereby affect synthesis of the lac metabolic enzymes1. The affinity of the repressor for operator DNA is decreased by binding inducer sugars and increased by binding anti-inducer sugars2. Based on regions of the primary structure implicated by genetic methods to be involved in sugar binding3–5, amino acid sequence homology between L-arabinose-binding protein (ABP) and lac repressor has recently been reported6. The sugar-binding sites for these two proteins might be expected to have similar structural features, as both bind L-arabinose and D-galactose. The high resolution structure of ABP reported in the accompanying article7 provides complete definition of amino acids in the sugar-binding site. By identification of homologous residues in the lac repressor, we have now predicted the structure of the portion of the repressor sugar-binding site which accommodates the galactosyl moiety. This prediction provides the first potential view of the inducer/anti-inducer site in the repressor protein.
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Sams, C., Vyas, N., Quiocho, F. et al. Predicted structure of the sugar-binding site of the lac repressor. Nature 310, 429–430 (1984). https://doi.org/10.1038/310429a0
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DOI: https://doi.org/10.1038/310429a0
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