EMD-38390

Single-particle
4.0 Å
EMD-38390
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Deposition: 20/12/2023
Map released: 14/08/2024
Last modified: 14/08/2024
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EMD-38390
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Cryo-EM structure of a frog VMAT2 in an apo conformation

EMD-38390

Single-particle
4.0 Å
EMD-38390
3D View Gallery
Deposition: 20/12/2023
Map released: 14/08/2024
Last modified: 14/08/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Xenopus laevis
Sample: XlVMAT2 WT
Fitted models: 8xiu

Deposition Authors: Lyu Y, Fu C, Ma H , Sun Z , Su Z, Zhou X
Engineering of a mammalian VMAT2 for cryo-EM analysis results in non-canonical protein folding.
Lyu Y, Fu C, Ma H , Su Z, Sun Z , Zhou X
(2024) Nat Commun , 15 , 6511 - 6511
PUBMED: 39095428
DOI: doi:10.1038/s41467-024-50934-5
ISSN: 2041-1723
Abstract:
Vesicular monoamine transporter 2 (VMAT2) belongs to the major facilitator superfamily (MFS), and mediates cytoplasmic monoamine packaging into presynaptic vesicles. Here, we present two cryo-EM structures of VMAT2, with a frog VMAT2 adopting a canonical MFS fold and an engineered sheep VMAT2 adopting a non-canonical fold. Both VMAT2 proteins mediate uptake of a selective fluorescent VMAT2 substrate into cells. Molecular docking, substrate binding and transport analysis reveal potential substrate binding mechanism in VMAT2. Meanwhile, caution is advised when interpreting engineered membrane protein structures.