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

Jani Reddy Bolla, Chih-Chia Su, Jared A. Delmar, Abhijith Radhakrishnan, Nitin Kumar, Tsung-Han Chou, Feng Long, Kanagalaghatta R. Rajashankar and Edward W. Yu ()
Additional contact information
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

Nature Communications, 2015, vol. 6, issue 1, 1-10

Abstract: 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.

Date: 2015
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/ncomms7874 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7874

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms7874

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().