8xiu

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Cryo-EM structure of a frog VMAT2 in an apo conformationCryo-EM structure of a frog VMAT2 in an apo conformation

Structural highlights

8xiu is a 1 chain structure with sequence from Xenopus laevis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 4Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

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.

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 Nat Commun. 2024 Aug 2;15(1):6511. doi: 10.1038/s41467-024-50934-5. PMID:39095428[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Lyu Y, Fu C, Ma H, Su Z, Sun Z, Zhou X. Engineering of a mammalian VMAT2 for cryo-EM analysis results in non-canonical protein folding. Nat Commun. 2024 Aug 2;15(1):6511. PMID:39095428 doi:10.1038/s41467-024-50934-5

8xiu, resolution 4.00Å

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OCA