title: Role of a conserved membrane glycine residue in a dicarboxylate transporter from Sinorhizobium meliloti.
abstract: Nitrogen-fixing rhizobial bacteroids import dicarboxylates by 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.
authors.affiliation: Institute of Biological Chemistry, Washington State University, Pullman, WA 99164-6340, USA.
authors.forename: Maria A
authors.initials: MA
authors.lastname: Trainer
authors.forename: Svetlana N
authors.initials: SN
authors.lastname: Yurgel
authors.forename: Michael L
authors.initials: ML
authors.lastname: Kahn
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D029382:Dicarboxylic Acid Transporters / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D005998:Glycine; D017433:Protein Structure, Secondary; D016962:Sinorhizobium meliloti / Q000378:metabolism*; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D019802:Succinic Acid / Q000378:metabolism; D013559:Symbiosis
chemical_list: D001426:Bacterial Proteins; D029382:Dicarboxylic Acid Transporters; C073786:dctA protein, Sinorhizobium meliloti; D019802:Succinic Acid; D005998:Glycine