Family resemblances: A common fold for some dimeric ion-coupled secondary transporters.

ABSTRACT: Membrane transporter proteins catalyze the passage of a broad range of solutes across cell membranes, allowing the uptake and efflux of crucial compounds. Because of the difficulty of expressing, purifying, and crystallizing integral membrane proteins, relatively few transporter structures have been elucidated to date. Although every membrane transporter has unique characteristics, structural and mechanistic similarities between evolutionarily diverse transporters have been identified. Here, we compare two recently reported structures of membrane proteins that act as antimicrobial efflux pumps, namely MtrF from Neisseria gonorrhoeae and YdaH from Alcanivorax borkumensis, both with each other and with the previously published structure of a sodium-dependent dicarboxylate transporter from Vi

SUBMITTER: Vergara-Jaque A 

PROVIDER: S-EPMC4621753 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature