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

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 hairpins that suggest a plausible pathway for substrate transport. Further analyses also suggest that YdaH could act as an antibiotic efflux pump and mediate bacterial resistance to sulfonamide antimetabolite drugs.
 [1] ;  [2] ;  [2] ;  [1] ;  [1] ;  [2] ;  [2] ;  [3] ;  [4]
  1. Iowa State Univ., IA (United States). Dept. of Chemistry
  2. Iowa State Univ., IA (United States). Dept. of Physics and Astronomy
  3. Argonne National Laboratory, IL (United States). NE-CAT and Dept. of chemistry and Chemical BIology
  4. Iowa State Univ., IA (United States). Dept. of Chemistry and Dept. of Physics and Astronomy
Publication Date:
Grant/Contract Number:
Accepted Manuscript
Journal Name:
Nature Communications
Additional Journal Information:
Journal Volume: 6; Journal ID: ISSN 2041-1723
Nature Publishing Group
Research Org:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22); National Institutes of Health (NIH)
Country of Publication:
United States
OSTI Identifier: