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8P97

BtuB3G3 bound to cyanocobalamin with disordered EL8

Summary for 8P97
Entry DOI10.2210/pdb8p97/pdb
EMDB information17574
DescriptorTonB-dependent receptor, Putative surface layer protein, CYANOCOBALAMIN (3 entities in total)
Functional Keywordscyanocobalamin, transporter, lipoprotein, complex, membrane protein
Biological sourceBacteroides thetaiotaomicron VPI-5482
More
Total number of polymer chains2
Total formula weight121412.78
Authors
Silale, A.,Abellon-Ruiz, J.,van den Berg, B. (deposition date: 2023-06-05, release date: 2023-08-16, Last modification date: 2023-09-20)
Primary citationAbellon-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: 37543597
DOI: 10.1038/s41467-023-40427-2
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.75 Å)
Structure validation

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