Dataset Information
Thermostabilized human prestin in complex with chloride, sulfate or salicylate
Ontology highlight
ABSTRACT:
SUBMITTER: Tsukasa Kusakizako
PROVIDER: EMPIAR-11199 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Cryo-EM structures of thermostabilized prestin provide mechanistic insights underlying outer hair cell electromotility.
Nature communications 20221020 1
Outer hair cell elecromotility, driven by prestin, is essential for mammalian cochlear amplification. Here, we report the cryo-EM structures of thermostabilized prestin (Pres<sup>TS</sup>), complexed with chloride, sulfate, or salicylate at 3.52-3.63 Å resolutions. The central positively-charged cavity allows flexible binding of various anion species, which likely accounts for the known distinct modulations of nonlinear capacitance (NLC) by different anions. Comparisons of these Pres<sup>TS</sup ...[more]
