7SUN

Atomic model of prestin from gerbil (Meriones unguiculatus)

Summary for 7SUN

• Entry DOI: 10.2210/pdb7sun/pdb
• EMDB information: 25442
• Descriptor: Prestin, Enhanced Yellow Fluorescent Protein chimera (1 entity in total)
• Functional Keywords: prestin (slc26a5), cochlear amplification, nonlinear capacitance, membrane protein, motor protein
• Biological source: Meriones unguiculatus (Mongolian jird, Gerbillus unguiculatus); More
• Total number of polymer chains: 2
• Total formula weight: 223731.61

Authors

Butan, C.,Santos-Sacchi, J. (deposition date: 2021-11-17, release date: 2022-01-12, Last modification date: 2024-02-28)

Primary citation

Butan, C.,Song, Q.,Bai, J.P.,Tan, W.J.T.,Navaratnam, D.,Santos-Sacchi, J.
Single particle cryo-EM structure of the outer hair cell motor protein prestin.
Nat Commun, 13:290-290, 2022

PubMed Abstract: The mammalian outer hair cell (OHC) protein prestin (Slc26a5) differs from other Slc26 family members due to its unique piezoelectric-like property that drives OHC electromotility, the putative mechanism for cochlear amplification. Here, we use cryo-electron microscopy to determine prestin's structure at 3.6 Å resolution. Prestin is structurally similar to the anion transporter Slc26a9. It is captured in an inward-open state which may reflect prestin's contracted state. Two well-separated transmembrane (TM) domains and two cytoplasmic sulfate transporter and anti-sigma factor antagonist (STAS) domains form a swapped dimer. The transmembrane domains consist of 14 transmembrane segments organized in two 7+7 inverted repeats, an architecture first observed in the bacterial symporter UraA. Mutation of prestin's chloride binding site removes salicylate competition with anions while retaining the prestin characteristic displacement currents (Nonlinear Capacitance), undermining the extrinsic voltage sensor hypothesis for prestin function.

PubMed: 35022426
DOI: 10.1038/s41467-021-27915-z

Experimental method

ELECTRON MICROSCOPY (3.6 Å)