7biz

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==Structure of a B12 binding lipoprotein from Bacteroides thetaiotaomicron==
==Structure of a B12 binding lipoprotein from Bacteroides thetaiotaomicron==
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<StructureSection load='7biz' size='340' side='right'caption='[[7biz]], [[Resolution|resolution]] 1.53&Aring;' scene=''>
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<StructureSection load='7biz' size='340' side='right'caption='[[7biz]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7biz]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BIZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BIZ FirstGlance]. <br>
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BIZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BIZ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=15P:POLYETHYLENE+GLYCOL+(N=34)'>15P</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CNC:CO-CYANOCOBALAMIN'>CNC</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7biz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7biz OCA], [https://pdbe.org/7biz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7biz RCSB], [https://www.ebi.ac.uk/pdbsum/7biz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7biz ProSAT]</span></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=7biz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7biz OCA], [https://pdbe.org/7biz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7biz RCSB], [https://www.ebi.ac.uk/pdbsum/7biz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7biz ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Human gut commensal Bacteroidetes rely on multiple transport systems to acquire vitamin B12 and related cobamides for fitness in the gut. In addition to a set of conserved transport proteins, these systems also include a diverse repertoire of additional proteins with unknown function. Here, we report the function and structural characterization of one of these proteins, BtuH, which binds vitamin B12 directly via a C-terminal globular domain that has no known structural homologs. This protein is required for efficient B12 transport and competitive fitness in the gut, demonstrating that members of the heterogeneous suite of accessory proteins encoded in Bacteroides cobamide transport system loci can play key roles in vitamin acquisition. IMPORTANCE The gut microbiome is a complex microbial community with important impacts on human health. One of the major groups within the gut microbiome, the Bacteroidetes, rely on their ability to capture vitamin B12 and related molecules for fitness in the gut. Unlike well-studied model organisms, gut Bacteroidetes genomes often include multiple vitamin B12 transport systems with a heterogeneous set of components. The role, if any, of these components was unknown. Here, we identify new proteins that play key roles in vitamin B12 capture in these organisms. Notably, these proteins are associated with some B12 transport systems and not others (even in the same bacterial strain), suggesting that these systems may assemble into functionally distinct machines to capture vitamin B12 and related molecules.
 
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Gut Commensal Bacteroidetes Encode a Novel Class of Vitamin B12-Binding Proteins.,Putnam EE, Abellon-Ruiz J, Killinger BJ, Rosnow JJ, Wexler AG, Folta-Stogniew E, Wright AT, van den Berg B, Goodman AL mBio. 2022 Mar 1:e0284521. doi: 10.1128/mbio.02845-21. PMID:35227073<ref>PMID:35227073</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 7biz" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Abellon-Ruiz, J]]
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[[Category: Abellon-Ruiz J]]
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[[Category: Berg, B van den]]
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[[Category: Van den Berg B]]
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[[Category: B12 binding protein]]
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[[Category: Lipoprotein]]
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[[Category: Unknown function]]
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Revision as of 14:43, 31 August 2022

Structure of a B12 binding lipoprotein from Bacteroides thetaiotaomicron

PDB ID 7biz

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