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5e7g

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==Crystal structure of Bacova_02650 with xylogluco-oligosaccharide==
==Crystal structure of Bacova_02650 with xylogluco-oligosaccharide==
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<StructureSection load='5e7g' size='340' side='right' caption='[[5e7g]], [[Resolution|resolution]] 2.37&Aring;' scene=''>
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<StructureSection load='5e7g' size='340' side='right'caption='[[5e7g]], [[Resolution|resolution]] 2.37&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5e7g]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E7G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E7G FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5e7g]] 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=5E7G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E7G FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=XYS:XYLOPYRANOSE'>XYS</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.37&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5e75|5e75]], [[5e76|5e76]], [[5e7h|5e7h]]</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=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=XYS:XYLOPYRANOSE'>XYS</scene></td></tr>
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<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=5e7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e7g OCA], [http://pdbe.org/5e7g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e7g RCSB], [http://www.ebi.ac.uk/pdbsum/5e7g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e7g 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=5e7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e7g OCA], [https://pdbe.org/5e7g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e7g RCSB], [https://www.ebi.ac.uk/pdbsum/5e7g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e7g ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/Y2650_BACO1 Y2650_BACO1]] Polysaccharide-binding protein present at the surface of the cell. Probably mediates xyloglucan-binding before xyloglucan transport in the periplasm for degradation.<ref>PMID:24463512</ref>
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[https://www.uniprot.org/uniprot/Y2650_BACO1 Y2650_BACO1] Polysaccharide-binding protein present at the surface of the cell. Probably mediates xyloglucan-binding before xyloglucan transport in the periplasm for degradation.<ref>PMID:24463512</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Polysaccharide utilization loci (PUL) within the genomes of resident human gut Bacteroidetes are central to the metabolism of the otherwise indigestible complex carbohydrates known as "dietary fiber." However, functional characterization of PUL lags significantly behind sequencing efforts, which limits physiological understanding of the human-bacterial symbiosis. In particular, the molecular basis of complex polysaccharide recognition, an essential prerequisite to hydrolysis by cell surface glycosidases and subsequent metabolism, is generally poorly understood. Here, we present the biochemical, structural, and reverse genetic characterization of two unique cell surface glycan-binding proteins (SGBPs) encoded by a xyloglucan utilization locus (XyGUL) from Bacteroides ovatus, which are integral to growth on this key dietary vegetable polysaccharide. Biochemical analysis reveals that these outer membrane-anchored proteins are in fact exquisitely specific for the highly branched xyloglucan (XyG) polysaccharide. The crystal structure of SGBP-A, a SusD homolog, with a bound XyG tetradecasaccharide reveals an extended carbohydrate-binding platform that primarily relies on recognition of the beta-glucan backbone. The unique, tetra-modular structure of SGBP-B is comprised of tandem Ig-like folds, with XyG binding mediated at the distal C-terminal domain. Despite displaying similar affinities for XyG, reverse-genetic analysis reveals that SGBP-B is only required for the efficient capture of smaller oligosaccharides, whereas the presence of SGBP-A is more critical than its carbohydrate-binding ability for growth on XyG. Together, these data demonstrate that SGBP-A and SGBP-B play complementary, specialized roles in carbohydrate capture by B. ovatus and elaborate a model of how vegetable xyloglucans are accessed by the Bacteroidetes IMPORTANCE: The Bacteroidetes are dominant bacteria in the human gut that are responsible for the digestion of the complex polysaccharides that constitute "dietary fiber." Although this symbiotic relationship has been appreciated for decades, little is currently known about how Bacteroidetes seek out and bind plant cell wall polysaccharides as a necessary first step in their metabolism. Here, we provide the first biochemical, crystallographic, and genetic insight into how two surface glycan-binding proteins from the complex Bacteroides ovatus xyloglucan utilization locus (XyGUL) enable recognition and uptake of this ubiquitous vegetable polysaccharide. Our combined analysis illuminates new fundamental aspects of complex polysaccharide recognition, cleavage, and import at the Bacteroidetes cell surface that may facilitate the development of prebiotics to target this phylum of gut bacteria.
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Molecular Dissection of Xyloglucan Recognition in a Prominent Human Gut Symbiont.,Tauzin AS, Kwiatkowski KJ, Orlovsky NI, Smith CJ, Creagh AL, Haynes CA, Wawrzak Z, Brumer H, Koropatkin NM MBio. 2016 Apr 26;7(2). pii: e02134-15. doi: 10.1128/mBio.02134-15. PMID:27118585<ref>PMID:27118585</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 5e7g" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Koropatkin, N M]]
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[[Category: Bacteroides ovatus ATCC 8483]]
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[[Category: Carbohydrate-binding protein]]
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[[Category: Large Structures]]
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[[Category: Sugar binding protein]]
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[[Category: Koropatkin NM]]

Current revision

Crystal structure of Bacova_02650 with xylogluco-oligosaccharide

PDB ID 5e7g

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