6LHR

Crystal structure of the complex between Vesicle Amine Transport-1 and NADP

Summary for 6LHR

• Entry DOI: 10.2210/pdb6lhr/pdb
• Descriptor: Synaptic vesicle membrane protein VAT-1 homolog, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• Functional Keywords: vat1, complex, quinone, oxidoreductase
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 4
• Total formula weight: 155189.92

Authors

Hakoshima, T.,Kim, S.-Y.,Mori, T. (deposition date: 2019-12-09, release date: 2021-01-20, Last modification date: 2023-11-22)

Primary citation

Kim, S.-Y.,Mori, T.,Chek, M.F.,Furuya, S.,Matsumoto, K.,Yajima, T.,Ogura, T.,Hakoshima, T.
Structural insights into vesicle amine transport-1 (VAT-1) as a member of the NADPH-dependent quinone oxidoreductase family.
Sci Rep, 11:2120-2120, 2021

PubMed Abstract: Vesicle amine transport protein-1 (VAT-1) has been implicated in the regulation of vesicular transport, mitochondrial fusion, phospholipid transport and cell migration, and is a potential target of anticancer drugs. Little is known about the molecular function of VAT-1. The amino acid sequence indicates that VAT-1 belongs to the quinone oxidoreductase subfamily, suggesting that VAT-1 may possess enzymatic activity in unknown redox processes. To clarify the molecular function of VAT-1, we determined the three-dimensional structure of human VAT-1 in the free state at 2.3 Å resolution and found that VAT-1 forms a dimer with the conserved NADPH-binding cleft on each protomer. We also determined the structure of VAT-1 in the NADP-bound state at 2.6 Å resolution and found that NADP binds the binding cleft to create a putative active site with the nicotine ring. Substrate screening suggested that VAT-1 possesses oxidoreductase activity against quinones such as 1,2-naphthoquinone and 9,10-phenanthrenequinone.

PubMed: 33483563
DOI: 10.1038/s41598-021-81409-y

Experimental method

X-RAY DIFFRACTION (2.62 Å)