6O84

Cryo-EM structure of OTOP3 from xenopus tropicalis

Summary for 6O84

• Entry DOI: 10.2210/pdb6o84/pdb
• EMDB information: 0650
• Descriptor: LOC100127796 protein,LOC100127796 protein,OTOP3,LOC100127796 protein,LOC100127796 protein (1 entity in total)
• Functional Keywords: otopetrin, proton, channel, membrane protein
• Biological source: Xenopus tropicalis (Western clawed frog); More
• Total number of polymer chains: 2
• Total formula weight: 146704.59

Authors

Chen, Q.F.,Bai, X.C.,Jiang, Y.X. (deposition date: 2019-03-08, release date: 2019-04-24, Last modification date: 2024-03-20)

Primary citation

Chen, Q.,Zeng, W.,She, J.,Bai, X.,Jiang, Y.
Structural and functional characterization of an otopetrin family proton channel.
Elife, 8:-, 2019

PubMed Abstract: 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.

PubMed: 30973323
DOI: 10.7554/eLife.46710

Experimental method

ELECTRON MICROSCOPY (3.92 Å)