8XIT

Cryo-EM structure of sheep VMAT2 dimer in an atypical fold

Summary for 8XIT

Entry DOI	10.2210/pdb8xit/pdb
EMDB information	38389
Descriptor	OaVMAT2-BRIL (1 entity in total)
Functional Keywords	vesicular monoamine transporter, slc18a2, mfs, apo, conformation, transport protein
Biological source	Ovis aries
Total number of polymer chains	2
Total formula weight	137185.38
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 Cited by 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 PDB entries with the same primary citation
Experimental method	ELECTRON MICROSCOPY (3.2 Å)

Structure validation