6TQF
The structure of ABC transporter Rv1819c in AMP-PNP bound state
Summary for 6TQF
| Entry DOI | 10.2210/pdb6tqf/pdb |
| Related | 6TQE |
| EMDB information | 10550 |
| Descriptor | ABC transporter ATP-binding protein/permease, DODECYL-BETA-D-MALTOSIDE, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | cobalamin, vitamin b12, abc transporter, exporter fold, import, tuberculosis, transport protein |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 2 |
| Total formula weight | 151011.15 |
| Authors | Rempel, S.,Gati, C.,Slotboom, D.J.,Guskov, A. (deposition date: 2019-12-16, release date: 2020-04-01, Last modification date: 2025-07-09) |
| Primary citation | Rempel, S.,Gati, C.,Nijland, M.,Thangaratnarajah, C.,Karyolaimos, A.,de Gier, J.W.,Guskov, A.,Slotboom, D.J. A mycobacterial ABC transporter mediates the uptake of hydrophilic compounds. Nature, 580:409-412, 2020 Cited by PubMed Abstract: Mycobacterium tuberculosis (Mtb) is an obligate human pathogen and the causative agent of tuberculosis. Although Mtb can synthesize vitamin B (cobalamin) de novo, uptake of cobalamin has been linked to pathogenesis of tuberculosis. Mtb does not encode any characterized cobalamin transporter; however, the gene rv1819c was found to be essential for uptake of cobalamin. This result is difficult to reconcile with the original annotation of Rv1819c as a protein implicated in the transport of antimicrobial peptides such as bleomycin. In addition, uptake of cobalamin seems inconsistent with the amino acid sequence, which suggests that Rv1819c has a bacterial ATP-binding cassette (ABC)-exporter fold. Here, we present structures of Rv1819c, which reveal that the protein indeed contains the ABC-exporter fold, as well as a large water-filled cavity of about 7,700 Å, which enables the protein to transport the unrelated hydrophilic compounds bleomycin and cobalamin. On the basis of these structures, we propose that Rv1819c is a multi-solute transporter for hydrophilic molecules, analogous to the multidrug exporters of the ABC transporter family, which pump out structurally diverse hydrophobic compounds from cells. PubMed: 32296172DOI: 10.1038/s41586-020-2072-8 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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