3HFX
Crystal structure of carnitine transporter
Summary for 3HFX
| Entry DOI | 10.2210/pdb3hfx/pdb |
| Descriptor | L-carnitine/gamma-butyrobetaine antiporter, MERCURY (II) ION, CARNITINE (3 entities in total) |
| Functional Keywords | helix-turn-helix, antiport, cell inner membrane, cell membrane, transmembrane, transport, transport protein |
| Biological source | Escherichia coli |
| Cellular location | Cell inner membrane; Multi-pass membrane protein: P31553 |
| Total number of polymer chains | 1 |
| Total formula weight | 59076.99 |
| Authors | Tang, L.,Wang, W.-H.,Bai, L.,Jiang, T. (deposition date: 2009-05-13, release date: 2010-03-31, Last modification date: 2024-03-20) |
| Primary citation | Tang, L.,Bai, L.,Wang, W.-H.,Jiang, T. Crystal structure of the carnitine transporter and insights into the antiport mechanism Nat.Struct.Mol.Biol., 17:492-496, 2010 Cited by PubMed Abstract: CaiT is a membrane antiporter that catalyzes the exchange of L-carnitine with gamma-butyrobetaine across the Escherichia coli membrane. To obtain structural insights into the antiport mechanism, we solved the crystal structure of CaiT at a resolution of 3.15 A. We crystallized CaiT as a homotrimer complex, in which each protomer contained 12 transmembrane helices and 4 l-carnitine molecules outlining the transport pathway across the membrane. Mutagenesis studies revealed a primary binding site at the center of the protein and a secondary substrate-binding site at the bottom of the intracellular vestibule. These results, together with the insights obtained from structural comparison with structurally homologous transporters, provide mechanistic insights into the association between substrate translocation and the conformational changes of CaiT. PubMed: 20357772DOI: 10.1038/nsmb.1788 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.15 Å) |
Structure validation
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