7EHL
Cryo-EM structure of human ABCB8 transporter in nucleotide binding state
Summary for 7EHL
| Entry DOI | 10.2210/pdb7ehl/pdb |
| EMDB information | 31142 |
| Descriptor | Mitochondrial potassium channel ATP-binding subunit, CHOLESTEROL, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total) |
| Functional Keywords | abc transporter, membrane protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 149864.37 |
| Authors | Li, S.J.,Yang, X.,Shen, Y.Q. (deposition date: 2021-03-29, release date: 2021-05-05, Last modification date: 2025-04-09) |
| Primary citation | Li, S.,Ren, Y.,Lu, X.,Shen, Y.,Yang, X. Cryo-EM structure of human ABCB8 transporter in nucleotide binding state. Biochem.Biophys.Res.Commun., 557:187-191, 2021 Cited by PubMed Abstract: Human ATP-binding cassette transporter 8 of subfamily B (hABCB8) is an ABC transporter that located in the inner membrane of mitochondria. The ABCB8 is involved in the maturation of Fe-S and protects the heart from oxidative stress. Here, we present the cryo-EM structure of human ABCB8 binding with AMPPNP in inward-facing conformation with resolution of 4.1 Å. hABCB8 shows an open-inward conformation when ATP is bound. Unexpectedly, cholesterol molecules were identified in the transmembrane domain of hABCB8. Our results provide structural basis for the transport mechanism of the ABC transporter in mitochondria. PubMed: 33872987DOI: 10.1016/j.bbrc.2021.04.007 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.1 Å) |
Structure validation
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