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J. Bacteriol. doi:10.1128/JB.01247-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Role of a conserved membrane glycine residue in a dicarboxylate transporter from Sinorhizobium meliloti

Institute of Biological Chemistry, Washington State University, Pullman, WA 99164-6340. USA; School of Molecular Biosciences, Washington State University, Pullman, WA 99164-6340. USA

^* To whom correspondence should be addressed. Email: kahn{at}wsu.edu.

	Abstract

Nitrogen-fixing rhizobial bacteroids import dicarboxylates using the DctA transporter. G114 of DctA is highly conserved. A G114D mutant is inactive but DctA with a small amino acid (G114A) or a helix disrupter (G114P) retains significant activity. G114 probably interacts with other membrane helices in stabilizing a substrate-binding pocket.