6FNP
Crystal structure of ECF-CbrT, a cobalamin transporter
Summary for 6FNP
| Entry DOI | 10.2210/pdb6fnp/pdb |
| Descriptor | Membrane protein, Energy-coupling factor transporter ATP-binding protein EcfA1, Energy-coupling factor transporter ATP-binding protein EcfA2, ... (4 entities in total) |
| Functional Keywords | vitamin b12, ecf transporter, membrane protein, cobalamin, abc transporter, transport protein |
| Biological source | Lactobacillus delbrueckii More |
| Total number of polymer chains | 8 |
| Total formula weight | 231014.50 |
| Authors | Santos, J.A.,Rempel, S.,Guskov, A.,Slotboom, D.J. (deposition date: 2018-02-05, release date: 2018-07-25, Last modification date: 2024-01-17) |
| Primary citation | Santos, J.A.,Rempel, S.,Mous, S.T.,Pereira, C.T.,Ter Beek, J.,de Gier, J.W.,Guskov, A.,Slotboom, D.J. Functional and structural characterization of an ECF-type ABC transporter for vitamin B12. Elife, 7:-, 2018 Cited by PubMed Abstract: Vitamin B12 (cobalamin) is the most complex B-type vitamin and is synthetized exclusively in a limited number of prokaryotes. Its biologically active variants contain rare organometallic bonds, which are used by enzymes in a variety of central metabolic pathways such as L-methionine synthesis and ribonucleotide reduction. Although its biosynthesis and role as co-factor are well understood, knowledge about uptake of cobalamin by prokaryotic auxotrophs is scarce. Here, we characterize a cobalamin-specific ECF-type ABC transporter from , ECF-CbrT, and demonstrate that it mediates the specific, ATP-dependent uptake of cobalamin. We solved the crystal structure of ECF-CbrT in an conformation to 3.4 Å resolution. Comparison with the ECF transporter for folate (ECF-FolT2) from the same organism, reveals how the identical ECF module adjusts to interact with the different substrate binding proteins FolT2 and CbrT. ECF-CbrT is unrelated to the well-characterized B12 transporter BtuCDF, but their biochemical features indicate functional convergence. PubMed: 29809140DOI: 10.7554/eLife.35828 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.4 Å) |
Structure validation
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