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| Title | Cryo-electron microscopy structure of human ABCB6 transporter. |
|---|---|
| Journal, issue, pages | Protein Sci, Vol. 29, Issue 12, Page 2363-2374, Year 2020 |
| Publish date | Oct 15, 2020 |
Authors | Chunyu Wang / Can Cao / Nan Wang / Xiangxi Wang / Xianping Wang / Xuejun C Zhang / ![]() |
| 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 ...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 links | Protein Sci / PubMed:33007128 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 4.0 - 5.2 Å |
| Structure data | EMDB-30609, PDB-7d7n: EMDB-30610, PDB-7d7r: |
| Source |
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Keywords | MEMBRANE PROTEIN / Transporter / Dimer / Porphyrins / Heme |
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