7EKL
Mitochondrial outer membrane protein
Summary for 7EKL
| Entry DOI | 10.2210/pdb7ekl/pdb |
| EMDB information | 31169 |
| Descriptor | ATP-binding cassette sub-family B member 6, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | mitochondrial outer membrane protein, membrane protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 189009.33 |
| Authors | Zhang, S.S. (deposition date: 2021-04-05, release date: 2021-08-25, Last modification date: 2024-06-05) |
| Primary citation | Song, G.,Zhang, S.,Tian, M.,Zhang, L.,Guo, R.,Zhuo, W.,Yang, M. Molecular insights into the human ABCB6 transporter. Cell Discov, 7:55-55, 2021 Cited by PubMed Abstract: ABCB6 plays a crucial role in energy-dependent porphyrin transport, drug resistance, toxic metal resistance, porphyrin biosynthesis, protection against stress, and encoding a blood group system Langereis antigen. However, the mechanism underlying porphyrin transport is still unclear. Here, we determined the cryo-electron microscopy (cryo-EM) structures of nanodisc-reconstituted human ABCB6 trapped in an apo-state and an ATP-bound state at resolutions of 3.6 and 3.5 Å, respectively. Our structures reveal a unique loop in the transmembrane domain (TMD) of ABCB6, which divides the TMD into two cavities. It restrains the access of substrates in the inward-facing state and is removed by ATP-driven conformational change. No ligand cavities were observed in the nucleotide-bound state, indicating a state following substrate release but prior to ATP hydrolysis. Structural analyses and functional characterizations suggest an "ATP-switch" model and further reveal the conformational changes of the substrate-binding pockets triggered by the ATP-driven regulation. PubMed: 34312373DOI: 10.1038/s41421-021-00284-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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