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TitleCryo-electron microscopy structure of human ABCB6 transporter.
Journal, issue, pagesProtein Sci, Vol. 29, Issue 12, Page 2363-2374, Year 2020
Publish dateOct 15, 2020
AuthorsChunyu Wang / Can Cao / Nan Wang / Xiangxi Wang / Xianping Wang / Xuejun C Zhang /
PubMed AbstractHuman 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 ...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.
External linksProtein Sci / PubMed:33007128 / PubMed Central
MethodsEM (single particle)
Resolution4.0 - 5.2 Å
Structure data

EMDB-30609, PDB-7d7n:
Cryo-EM structure of human ABCB6 transporter
Method: EM (single particle) / Resolution: 5.2 Å

EMDB-30610, PDB-7d7r:
Cryo-EM structure of the core domain of human ABCB6 transporter
Method: EM (single particle) / Resolution: 4.0 Å

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / Transporter / Dimer / Porphyrins / Heme

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