Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	BtuB TonB-dependent transporters and BtuG surface lipoproteins form stable complexes for vitamin B uptake in gut Bacteroides.
Journal, issue, pages	Nat Commun, Vol. 14, Issue 1, Page 4714, Year 2023
Publish date	Aug 5, 2023
Authors	Javier Abellon-Ruiz / Kalyanashis Jana / Augustinas Silale / Andrew M Frey / Arnaud Baslé / Matthias Trost / Ulrich Kleinekathöfer / Bert van den Berg /
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 ...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.
External links	Nat Commun / PubMed:37543597 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	1.33 - 3.72 Å
Structure data	16114 8blw EMDB-16114, PDB-8blw: Vitamin B12 transporter BtuB1 with lipoprotein BtuG1 from B. theta Method: EM (single particle) / Resolution: 3.22 Å 17574 8p97 EMDB-17574, PDB-8p97: BtuB3G3 bound to cyanocobalamin with disordered EL8 Method: EM (single particle) / Resolution: 2.75 Å 17575 8p98 EMDB-17575, PDB-8p98: BtuB3G3 bound to cyanocobalamin with ordered EL8 Method: EM (single particle) / Resolution: 2.97 Å PDB-8bmx: Bacteroides thetaiotaomicron B12 TonB dependent transporter in complex with a surface lipoprotein Method: X-RAY DIFFRACTION / Resolution: 3.72 Å PDB-8bmy: Bacteroides thetaiotaomicron surface lipoprotein bound to cyanocobalamin Method: X-RAY DIFFRACTION / Resolution: 1.72 Å PDB-8bmz: Bacteroides thetaiotaomicron surface lipoprotein BT1954 bound to adenosylcobalamin Method: X-RAY DIFFRACTION / Resolution: 2.3 Å PDB-8bn0: Bacteroides thetaiotaomicron surface protein BT1954 bound to Method: X-RAY DIFFRACTION / Resolution: 1.33 Å PDB-8okv: lipoprotein BT2095 from Bacteroides thetaiotamicron bound to cyanocobalamin CnCbl Method: X-RAY DIFFRACTION / Resolution: 2.6 Å
Chemicals	ChemComp-GAL: beta-D-galactopyranose / Galactose ChemComp-CNC: CYANOCOBALAMIN / Cyanocobalamin ChemComp-CL: Unknown entry / Chloride ChemComp-SO4: SULFATE ION / Sulfate ChemComp-HOH: WATER / Water ChemComp-B1Z: Adenosylcobalamin / medicationYM / Adenosylcobalamin ChemComp-CYN: CYANIDE ION / Cyanide ChemComp-CBY*: COB(II)INAMIDE
Source	bacteroides thetaiotaomicron vpi-5482 (bacteria)
Keywords	MEMBRANE PROTEIN / Outer membrane / TonB-dependent transporter / vitamin B12 / lipoprotein / Vitamin B12 Transport Complex Outer membrane / beta propeller surface protein B12 binding protein / Beta propeller Vitamin B12 binding Surface protein / Surface exposed protein Beta propeller Vitamin B12 binding protein / membrane associated / beta propeller / B12 binding protein / Cyanocobalamin / transporter / complex