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Cryo-EM structure of human TMEM45B with a bound GM3 (18:1;O2/24:1)
Mariana Grieben1, Julica Inderhees2, Niklas Ebersberger1
1Institute of Biochemistry, Center of Structural and Cell Biology in Medicine, University of Lübeck, 23562 Lübeck, Germany.
Abstract:
The orphan transmembrane protein 45B (TMEM45B) has been reported to be involved in mechanical pain hypersensitivity, antiviral processes, and cancer. The structure of human TMEM45B with bound monosialodihexosylganglioside (GM3, 18:1;O2/24:1), presented here, determined by single-particle cryo-electron microscopy (cryo-EM) to 2.8 Å, reveals a homotetrameric assembly of seven-transmembrane-helix protomers. The first six transmembrane helices from each protomer create a central hydrophobic tunnel that accommodates metal ions and the C24:1 fatty acid component of the ganglioside GM3.
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