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Yorodumi- PDB-8bmx: Bacteroides thetaiotaomicron B12 TonB dependent transporter in co... -
+Open data
-Basic information
Entry | Database: PDB / ID: 8bmx | ||||||
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Title | Bacteroides thetaiotaomicron B12 TonB dependent transporter in complex with a surface lipoprotein | ||||||
Components |
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Keywords | MEMBRANE PROTEIN / Vitamin B12 Transport Complex Outer membrane | ||||||
Function / homology | Function and homology information siderophore transmembrane transport / siderophore uptake transmembrane transporter activity / cell outer membrane Similarity search - Function | ||||||
Biological species | Bacteroides thetaiotaomicron VPI-5482 (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.72 Å | ||||||
Authors | Abellon-Ruiz, J. / Jana, K. / Silale, A. / Basle, A. / Kleinekathofer, U. / van den Berg, B. | ||||||
Funding support | United Kingdom, 1items
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Citation | Journal: Nat Commun / Year: 2023 Title: BtuB TonB-dependent transporters and BtuG surface lipoproteins form stable complexes for vitamin B uptake in gut Bacteroides. Authors: Javier Abellon-Ruiz / Kalyanashis Jana / Augustinas Silale / Andrew M Frey / Arnaud Baslé / Matthias Trost / Ulrich Kleinekathöfer / Bert van den Berg / 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. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8bmx.cif.gz | 1.4 MB | Display | PDBx/mmCIF format |
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PDB format | pdb8bmx.ent.gz | 994.4 KB | Display | PDB format |
PDBx/mmJSON format | 8bmx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8bmx_validation.pdf.gz | 497.7 KB | Display | wwPDB validaton report |
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Full document | 8bmx_full_validation.pdf.gz | 564.7 KB | Display | |
Data in XML | 8bmx_validation.xml.gz | 102.3 KB | Display | |
Data in CIF | 8bmx_validation.cif.gz | 135.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bm/8bmx ftp://data.pdbj.org/pub/pdb/validation_reports/bm/8bmx | HTTPS FTP |
-Related structure data
Related structure data | 8blwC 8bmyC 8bmzC 8bn0C 8okvC 8p97C 8p98C 1nqeS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
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