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

Trainer, Maria A; Yurgel, Svetlana N; Kahn, Michael L

Trainer, Maria A; Yurgel, Svetlana N; Kahn, Michael L.

Affiliation

Trainer MA; Institute of Biological Chemistry, Washington State University, Pullman, WA 99164-6340, USA.

J Bacteriol ; 189(5): 2160-3, 2007 Mar.

Article in En | MEDLINE | ID: mdl-17158675

ABSTRACT

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.

Subject(s)

Bacterial Proteins/chemistry; Dicarboxylic Acid Transporters/chemistry; Sinorhizobium meliloti/metabolism; Bacterial Proteins/genetics; Bacterial Proteins/physiology; Dicarboxylic Acid Transporters/genetics; Dicarboxylic Acid Transporters/physiology; Glycine; Protein Structure, Secondary; Structure-Activity Relationship; Substrate Specificity; Succinic Acid/metabolism; Symbiosis

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Sinorhizobium meliloti / Dicarboxylic Acid Transporters Language: En Journal: J Bacteriol Year: 2007 Type: Article Affiliation country: United States

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