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

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Listed:
  • Jani Reddy Bolla

    (Iowa State University)

  • Chih-Chia Su

    (Iowa State University)

  • Jared A. Delmar

    (Iowa State University)

  • Abhijith Radhakrishnan

    (Iowa State University)

  • Nitin Kumar

    (Iowa State University)

  • Tsung-Han Chou

    (Iowa State University)

  • Feng Long

    (Iowa State University)

  • Kanagalaghatta R. Rajashankar

    (Cornell University)

  • Edward W. Yu

    (Iowa State University
    Iowa State University)

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 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.

Suggested Citation

  • Jani Reddy Bolla & Chih-Chia Su & Jared A. Delmar & Abhijith Radhakrishnan & Nitin Kumar & Tsung-Han Chou & Feng Long & Kanagalaghatta R. Rajashankar & Edward W. Yu, 2015. "Crystal structure of the Alcanivorax borkumensis YdaH transporter reveals an unusual topology," Nature Communications, Nature, vol. 6(1), pages 1-10, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7874
    DOI: 10.1038/ncomms7874
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    Cited by:

    1. Benedikt T. Kuhn & Jonathan Zöller & Iwan Zimmermann & Tim Gemeinhardt & Dogukan H. Özkul & Julian D. Langer & Markus A. Seeger & Eric R. Geertsma, 2024. "Interdomain-linkers control conformational transitions in the SLC23 elevator transporter UraA," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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