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TitleCryo-EM structures of thermostabilized prestin provide mechanistic insights underlying outer hair cell electromotility.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 6208, Year 2022
Publish dateOct 20, 2022
AuthorsHaon Futamata / Masahiro Fukuda / Rie Umeda / Keitaro Yamashita / Atsuhiro Tomita / Satoe Takahashi / Takafumi Shikakura / Shigehiko Hayashi / Tsukasa Kusakizako / Tomohiro Nishizawa / Kazuaki Homma / Osamu Nureki /
PubMed AbstractOuter hair cell elecromotility, driven by prestin, is essential for mammalian cochlear amplification. Here, we report the cryo-EM structures of thermostabilized prestin (Pres), complexed with ...Outer hair cell elecromotility, driven by prestin, is essential for mammalian cochlear amplification. Here, we report the cryo-EM structures of thermostabilized prestin (Pres), 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 structures with recent prestin structures suggest rigid-body movement between the core and gate domains, and provide mechanistic insights into prestin inhibition by salicylate. Mutations at the dimeric interface severely diminished NLC, suggesting that stabilization of the gate domain facilitates core domain movement, thereby contributing to the expression of NLC. These findings advance our understanding of the molecular mechanism underlying mammalian cochlear amplification.
External linksNat Commun / PubMed:36266333 / PubMed Central
MethodsEM (single particle)
Resolution3.52 - 3.63 Å
Structure data

31757

7v73

EMDB-31757, PDB-7v73:
Thermostabilized human prestin in complex with chloride
Method: EM (single particle) / Resolution: 3.52 Å

31758

7v74

EMDB-31758, PDB-7v74:
Thermostabilized human prestin in complex with sulfate
Method: EM (single particle) / Resolution: 3.63 Å

31759

7v75

EMDB-31759, PDB-7v75:
Thermostabilized human prestin in complex with salicylate
Method: EM (single particle) / Resolution: 3.57 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-CLR:
CHOLESTEROL

ChemComp-LBN:
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine / phospholipid*YM

ChemComp-SO4:
SULFATE ION

ChemComp-SAL:
2-HYDROXYBENZOIC ACID

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / motor protein / prestin / SLC26A5 / electromotility

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