8XIU

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

Summary for 8XIU

• Entry DOI: 10.2210/pdb8xiu/pdb
• EMDB information: 38390
• Descriptor: XlVMAT2 (1 entity in total)
• Functional Keywords: vesicular monoamine transporter, slc18a2, mfs, fold, transport protein
• Biological source: Xenopus laevis
• Total number of polymer chains: 1
• Total formula weight: 55624.98

Authors

Lyu, Y.,Fu, C.,Ma, H.,Sun, Z.,Su, Z.,Zhou, X. (deposition date: 2023-12-20, release date: 2024-08-14)

Primary citation

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, 15:6511-6511, 2024

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 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.

PubMed: 39095428
DOI: 10.1038/s41467-024-50934-5

Experimental method

ELECTRON MICROSCOPY (4 Å)