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-Structure paper
Title | Engineering of a mammalian VMAT2 for cryo-EM analysis results in non-canonical protein folding. |
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Journal, issue, pages | Nat Commun, Vol. 15, Issue 1, Page 6511, Year 2024 |
Publish date | Aug 2, 2024 |
Authors | Ying Lyu / Chunting Fu / Haiyun Ma / Zhaoming Su / Ziyi Sun / Xiaoming Zhou / |
PubMed 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 ...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. |
External links | Nat Commun / PubMed:39095428 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.2 - 4.0 Å |
Structure data | EMDB-38389, PDB-8xit: EMDB-38390, PDB-8xiu: |
Source |
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Keywords | TRANSPORT PROTEIN / Vesicular monoamine transporter / SLC18A2 / MFS / Apo / Conformation / fold |