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| <StructureSection load='6e60' size='340' side='right'caption='[[6e60]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='6e60' size='340' side='right'caption='[[6e60]], [[Resolution|resolution]] 1.50Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6e60]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baco1 Baco1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E60 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E60 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6e60]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_ovatus_ATCC_8483 Bacteroides ovatus ATCC 8483]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E60 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6dmf|6dmf]]</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BACOVA_02743 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=411476 BACO1])</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=6e60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e60 OCA], [https://pdbe.org/6e60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e60 RCSB], [https://www.ebi.ac.uk/pdbsum/6e60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e60 ProSAT]</span></td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6e60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e60 OCA], [http://pdbe.org/6e60 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e60 RCSB], [http://www.ebi.ac.uk/pdbsum/6e60 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e60 ProSAT]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/A7LY27_BACO1 A7LY27_BACO1] |
| The human gut microbiota, which underpins nutrition and systemic health, is compositionally sensitive to the availability of complex carbohydrates in the diet. The Bacteroidetes comprise a dominant phylum in the human gut microbiota whose members thrive on dietary and endogenous glycans by employing a diversity of highly specific, multi-gene polysaccharide utilization loci (PUL), which encode a variety of carbohydrases, transporters, and sensor/regulators. PULs invariably also encode surface glycan-binding proteins (SGBPs) that play a central role in saccharide capture at the outer membrane. Here, we present combined biophysical, structural, and in vivo characterization of the two SGBPs encoded by the Bacteroides ovatus mixed-linkage beta-glucan utilization locus (MLGUL), thereby elucidating their key roles in the metabolism of this ubiquitous dietary cereal polysaccharide. In particular, molecular insight gained through several crystallographic complexes of SGBP-A and SGBP-B with oligosaccharides reveals that unique shape complementarity of binding platforms underpins specificity for the kinked MLG backbone vis-a-vis linear beta-glucans. Reverse-genetic analysis revealed that both the presence and binding ability of the SusD homolog BoSGBPMLG-A are essential for growth on MLG, whereas the divergent, multi-domain BoSGBPMLG-B is dispensable but may assist in oligosaccharide scavenging from the environment. The synthesis of these data illuminates the critical role SGBPs play in concert with other MLGUL components, reveals new structure-function relationships among SGBPs, and provides fundamental knowledge to inform future (meta)genomic, biochemical, and microbiological analyses of the human gut microbiota.
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| Surface glycan-binding proteins are essential for cereal beta-glucan utilization by the human gut symbiont Bacteroides ovatus.,Tamura K, Foley MH, Gardill BR, Dejean G, Schnizlein M, Bahr CME, Louise Creagh A, van Petegem F, Koropatkin NM, Brumer H Cell Mol Life Sci. 2019 May 6. pii: 10.1007/s00018-019-03115-3. doi:, 10.1007/s00018-019-03115-3. PMID:31062073<ref>PMID:31062073</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
| |
| <div class="pdbe-citations 6e60" style="background-color:#fffaf0;"></div>
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| == References ==
| |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Baco1]] | | [[Category: Bacteroides ovatus ATCC 8483]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Brumer, H]] | | [[Category: Brumer H]] |
| [[Category: Gardill, B R]] | | [[Category: Gardill BR]] |
| [[Category: Petegem, F Van]]
| | [[Category: Tamura K]] |
| [[Category: Tamura, K]] | | [[Category: Van Petegem F]] |
| [[Category: Binding protein]] | |
| [[Category: Outer membrane protein]]
| |
| [[Category: Sugar binding protein]]
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| [[Category: Tetratricopeptide repeat]]
| |
