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6QPI

Cryo-EM structure of calcium-free mTMEM16F lipid scramblase in nanodisc

Summary for 6QPI
Entry DOI10.2210/pdb6qpi/pdb
EMDB information4614
DescriptorAnoctamin-6 (1 entity in total)
Functional Keywordsmembrane protein, lipid scrambles, tmem16
Biological sourceMus musculus (Mouse)
Total number of polymer chains2
Total formula weight212735.45
Authors
Alvadia, C.,Lim, N.K.,Clerico Mosina, V.,Oostergetel, G.T.,Dutzler, R.,Paulino, C. (deposition date: 2019-02-14, release date: 2019-03-06, Last modification date: 2024-05-15)
Primary citationAlvadia, C.,Lim, N.K.,Clerico Mosina, V.,Oostergetel, G.T.,Dutzler, R.,Paulino, C.
Cryo-EM structures and functional characterization of the murine lipid scramblase TMEM16F.
Elife, 8:-, 2019
Cited by
PubMed Abstract: The lipid scramblase TMEM16F initiates blood coagulation by catalyzing the exposure of phosphatidylserine in platelets. The protein is part of a family of membrane proteins, which encompasses calcium-activated channels for ions and lipids. Here, we reveal features of murine TMEM16F (mTMEM16F) that underlie its function as a lipid scramblase and an ion channel. The cryo-EM data of mTMEM16F in absence and presence of Ca define the ligand-free closed conformation of the protein and the structure of a Ca-bound intermediate. Both conformations resemble their counterparts of the scrambling-incompetent anion channel mTMEM16A, yet with distinct differences in the region of ion and lipid permeation. In conjunction with functional data, we demonstrate the relationship between ion conduction and lipid scrambling. Although activated by a common mechanism, both functions appear to be mediated by alternate protein conformations that are at equilibrium in the ligand-bound state.
PubMed: 30785399
DOI: 10.7554/eLife.44365
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.3 Å)
Structure validation

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