7D7N

Cryo-EM structure of human ABCB6 transporter

Summary for 7D7N

• Entry DOI: 10.2210/pdb7d7n/pdb
• EMDB information: 30609
• Descriptor: ATP-binding cassette sub-family B member 6, mitochondrial (1 entity in total)
• Functional Keywords: transporter, dimer, porphyrins, heme, membrane protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 187948.34

Authors

Wang, C.,Cao, C.,Wang, N.,Wang, X.,Zhang, X.C. (deposition date: 2020-10-05, release date: 2020-10-21, Last modification date: 2024-03-27)

Primary citation

Wang, C.,Cao, C.,Wang, N.,Wang, X.,Wang, X.,Zhang, X.C.
Cryo-electron microscopy structure of human ABCB6 transporter.
Protein Sci., 29:2363-2374, 2020

PubMed Abstract: Human ATP-binding cassette transporter 6 of subfamily B (ABCB6) is an ABC transporter involved in the translocation toxic metals and anti-cancer drugs. Using cryo-electron microscopy, we determined the molecular structure of full-length ABCB6 in an apo state. The structure of ABCB6 unravels the architecture of a full-length ABCB transporter that harbors two N-terminal transmembrane domains which is indispensable for its ATPase activity in our in vitro assay. A slit-like substrate binding pocket of ABCB6 may accommodate the planar shape of porphyrins, and the existence of a secondary cavity near the mitochondrial intermembrane space side would further facilitate substrate release. Furthermore, the ATPase activity of ABCB6 stimulated with a variety of porphyrin substrates showed different profiles in the presence of glutathione (GSH), suggesting the action of a distinct substrate translocation mechanism depending on the use of GSH as a cofactor.

PubMed: 33007128
DOI: 10.1002/pro.3960

Experimental method

ELECTRON MICROSCOPY (5.2 Å)