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Methionine-binding protein, best exemplified by the bacterial protein MetQ, is a periplasmic substrate-binding protein integral to the high-affinity import of methionine via the MetNIQ ATP-binding cassette (ABC) transporter system in a wide range of bacteria.[2][5] MetQ binds both L- and D-methionine, undergoing a Venus flytrap-type conformational change, and delivers the amino acid to the membrane-spanning transporter MetNI, which couples ATP hydrolysis to methionine uptake into the bacterial cell.[2][5] These proteins are critical for bacterial survival and virulence in environments where methionine is limiting. Although not drug targets in humans, methionine-binding proteins are potential targets for antimicrobial development via transporter inhibition as they represent an essential system for amino acid scavenging in bacteria.[2][5] There are no direct human homologs with transporter function, but functionally related amino acid-binding and shuttling proteins exist across organisms for methionine homeostasis.
Competitive inhibition of methionine transport (for theoretical or experimental inhibitors)
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