8p98

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m (Protected "8p98" [edit=sysop:move=sysop])
Current revision (08:29, 16 August 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 8p98 is ON HOLD until Paper Publication
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==BtuB3G3 bound to cyanocobalamin with ordered EL8==
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<StructureSection load='8p98' size='340' side='right'caption='[[8p98]], [[Resolution|resolution]] 2.97&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8p98]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron_VPI-5482 Bacteroides thetaiotaomicron VPI-5482]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8P98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8P98 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.97&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CNC:CO-CYANOCOBALAMIN'>CNC</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8p98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8p98 OCA], [https://pdbe.org/8p98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8p98 RCSB], [https://www.ebi.ac.uk/pdbsum/8p98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8p98 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A0P0F201_BACT4 A0A0P0F201_BACT4]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Vitamin B(12) (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(12) outer membrane transporters together with a conserved array of surface-exposed B(12)-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(12) with high affinities. Closing of the BtuG lid following B(12) capture causes destabilisation of the bound B(12) 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.
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Authors:
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BtuB TonB-dependent transporters and BtuG surface lipoproteins form stable complexes for vitamin B(12) uptake in gut Bacteroides.,Abellon-Ruiz J, Jana K, Silale A, Frey AM, Basle A, Trost M, Kleinekathofer U, van den Berg B Nat Commun. 2023 Aug 5;14(1):4714. doi: 10.1038/s41467-023-40427-2. PMID:37543597<ref>PMID:37543597</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 8p98" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bacteroides thetaiotaomicron VPI-5482]]
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[[Category: Large Structures]]
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[[Category: Abellon-Ruiz J]]
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[[Category: Silale A]]
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[[Category: Van den Berg B]]

Current revision

BtuB3G3 bound to cyanocobalamin with ordered EL8

PDB ID 8p98

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