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TitleStructural and functional characterization of an otopetrin family proton channel.
Journal, issue, pagesElife, Vol. 8, Year 2019
Publish dateApr 11, 2019
AuthorsQingfeng Chen / Weizhong Zeng / Ji She / Xiao-Chen Bai / Youxing Jiang /
PubMed AbstractThe otopetrin (OTOP) proteins were recently characterized as proton channels. Here we present the cryo-EM structure of OTOP3 from (XtOTOP3) along with functional characterization of the channel. ...The otopetrin (OTOP) proteins were recently characterized as proton channels. Here we present the cryo-EM structure of OTOP3 from (XtOTOP3) along with functional characterization of the channel. XtOTOP3 forms a homodimer with each subunit containing 12 transmembrane helices that can be divided into two structurally homologous halves; each half assembles as an α-helical barrel that could potentially serve as a proton conduction pore. Both pores open from the extracellular half before becoming occluded at a central constriction point consisting of three highly conserved residues - Gln-Asp/Asn-Tyr (the constriction triads). Mutagenesis shows that the constriction triad from the second pore is less amenable to perturbation than that of the first pore, suggesting an unequal contribution between the two pores to proton transport. We also identified several key residues at the interface between the two pores that are functionally important, particularly Asp509, which confers intracellular pH-dependent desensitization to OTOP channels.
External linksElife / PubMed:30973323 / PubMed Central
MethodsEM (single particle)
Resolution3.92 Å
Structure data

0650

6o84

EMDB-0650, PDB-6o84:
Cryo-EM structure of OTOP3 from xenopus tropicalis
Method: EM (single particle) / Resolution: 3.92 Å

Source
  • xenopus tropicalis (tropical clawed frog)
KeywordsMEMBRANE PROTEIN / Otopetrin / proton / channel

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