Biochemistry Residues in the pathway through a membrane transporter (biological transport/cysteine scanning mutagenesis/membrane protein structure/membrane carrier/translocation pathway) ABSTRACT The structure of solute transporters is understood largely from analysis of their amino acid sequences, and more direct information is greatly needed. Here we report work that applies cysteine scanning mutagenesis to describe structure-function relations in UhpT, a bacterial membrane transporter. By using an impermeant SH-reactive agent to probe single-cysteine variants, we show that UhpT transmem-brane segment 7 spans the membrane as an a-helix and that the central portion of this helix is exposed to both membrane surfaces, forming part of the translocation pathway through this transporter. Membrane carriers and transporters comprise a large and diverse collection of proteins with functions directed to the regulation of ion and solute flux across cell membranes (1-5). Accordingly, such proteins occupy central positions in cellular programs that range from nutrient accumulation by bacteria to
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