4R0C

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

Summary for 4R0C

• Entry DOI: 10.2210/pdb4r0c/pdb
• Descriptor: AbgT putative transporter family, SODIUM ION, DODECYL-BETA-D-MALTOSIDE, ... (5 entities in total)
• Functional Keywords: transmembrane protein, membrane protein
• Biological source: Alcanivorax borkumensis SK2
• Total number of polymer chains: 4
• Total formula weight: 210735.81

Authors

Su, C.-C.,Bolla, J.R.,Yu, E.W. (deposition date: 2014-07-30, release date: 2015-04-29, Last modification date: 2024-02-28)

Primary citation

Bolla, J.R.,Su, C.C.,Delmar, J.A.,Radhakrishnan, A.,Kumar, N.,Chou, T.H.,Long, F.,Rajashankar, K.R.,Yu, E.W.
Crystal structure of the Alcanivorax borkumensis YdaH transporter reveals an unusual topology.
Nat Commun, 6:6874-6874, 2015

PubMed 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.

PubMed: 25892120
DOI: 10.1038/ncomms7874

Experimental method

X-RAY DIFFRACTION (2.963 Å)