8BMX
Bacteroides thetaiotaomicron B12 TonB dependent transporter in complex with a surface lipoprotein
Summary for 8BMX
| Entry DOI | 10.2210/pdb8bmx/pdb |
| Descriptor | Putative TonB-linked outer membrane receptor, YncE family protein (2 entities in total) |
| Functional Keywords | vitamin b12 transport complex outer membrane, membrane protein |
| Biological source | Bacteroides thetaiotaomicron VPI-5482 More |
| Total number of polymer chains | 6 |
| Total formula weight | 365968.54 |
| Authors | Abellon-Ruiz, J.,Jana, K.,Silale, A.,Basle, A.,Kleinekathofer, U.,van den Berg, B. (deposition date: 2022-11-11, release date: 2023-09-20) |
| Primary citation | Abellon-Ruiz, J.,Jana, K.,Silale, A.,Frey, A.M.,Basle, A.,Trost, M.,Kleinekathofer, U.,van den Berg, B. BtuB TonB-dependent transporters and BtuG surface lipoproteins form stable complexes for vitamin B 12 uptake in gut Bacteroides. Nat Commun, 14:4714-4714, 2023 Cited by PubMed Abstract: Vitamin B (cobalamin) is required for most human gut microbes, many of which are dependent on scavenging to obtain this vitamin. Since bacterial densities in the gut are extremely high, competition for this keystone micronutrient is severe. Contrasting with Enterobacteria, members of the dominant genus Bacteroides often encode several BtuB vitamin B outer membrane transporters together with a conserved array of surface-exposed B-binding lipoproteins. Here we show that the BtuB transporters from Bacteroides thetaiotaomicron form stable, pedal bin-like complexes with surface-exposed BtuG lipoprotein lids, which bind B with high affinities. Closing of the BtuG lid following B capture causes destabilisation of the bound B by a conserved BtuB extracellular loop, causing translocation of the vitamin to BtuB and subsequent transport. We propose that TonB-dependent, lipoprotein-assisted small molecule uptake is a general feature of Bacteroides spp. that is important for the success of this genus in colonising the human gut. PubMed: 37543597DOI: 10.1038/s41467-023-40427-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.72 Å) |
Structure validation
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