Molecular architecture and the structural basis for anion interaction in prestin and SLC26 transporters

Dmitry Gorbunov, Mattia Sturlese, Florian Nies, Murielle Kluge, Massimo Bellanda, Roberto Battistutta and Dominik Oliver ()
Additional contact information
Dmitry Gorbunov: Institute of Physiology and Pathophysiology, Philipps University
Mattia Sturlese: University of Padua, via Marzolo 1
Florian Nies: Institute of Physiology and Pathophysiology, Philipps University
Murielle Kluge: Institute of Physiology and Pathophysiology, Philipps University
Massimo Bellanda: University of Padua, via Marzolo 1
Roberto Battistutta: University of Padua, via Marzolo 1
Dominik Oliver: Institute of Physiology and Pathophysiology, Philipps University

Nature Communications, 2014, vol. 5, issue 1, 1-13

Abstract: Abstract Prestin (SLC26A5) is a member of the SLC26/SulP anion transporter family. Its unique quasi-piezoelectric mechanical activity generates fast cellular motility of cochlear outer hair cells, a key process underlying active amplification in the mammalian ear. Despite its established physiological role, it is essentially unknown how prestin can generate mechanical force, since structural information on SLC26/SulP proteins is lacking. Here we derive a structural model of prestin and related transporters by combining homology modelling, MD simulations and cysteine accessibility scanning. Prestin’s transmembrane core region is organized in a 7+7 inverted repeat architecture. The model suggests a central cavity as the substrate-binding site located midway of the anion permeation pathway, which is supported by experimental solute accessibility and mutational analysis. Anion binding to this site also controls the electromotile activity of prestin. The combined structural and functional data provide a framework for understanding electromotility and anion transport by SLC26 transporters.

Date: 2014
References: Add references at CitEc
Citations: View citations in EconPapers (3)

Downloads: (external link)
https://www.nature.com/articles/ncomms4622 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:5:y:2014:i:1:d:10.1038_ncomms4622

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

DOI: 10.1038/ncomms4622

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 ().