Crystal structure of the Alcanivorax borkumensis YdaH transporter reveals an unusual topology.

ABSTRACT: The potential of the folic acid biosynthesis pathway as a target for the development of antibiotics has been clinically validated. However, many pathogens have developed resistance to these antibiotics, prompting a re-evaluation of potential drug targets within the pathway. The ydaH gene of Alcanivorax borkumensis encodes an integral membrane protein of the AbgT family of transporters for which no structural information was available. Here we report the crystal structure of A. borkumensis YdaH, revealing a dimeric molecule with an architecture distinct from other families of transporters. YdaH is a bowl-shaped dimer with a solvent-filled basin extending from the cytoplasm to halfway across the membrane bilayer. Each subunit of the transporter contains nine transmembrane helices and two hai

SUBMITTER: Bolla JR 

PROVIDER: S-EPMC4410182 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature