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7kv4

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Current revision (14:58, 6 March 2024) (edit) (undo)
 
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<StructureSection load='7kv4' size='340' side='right'caption='[[7kv4]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
<StructureSection load='7kv4' size='340' side='right'caption='[[7kv4]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7kv4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_fluxus_dsm_22534 Bacteroides fluxus dsm 22534]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KV4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KV4 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7kv4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_fluxus_YIT_12057 Bacteroides fluxus YIT 12057]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KV4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KV4 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HMPREF9446_00614 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=763034 Bacteroides fluxus DSM 22534])</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]] 1.84&#8491;</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=7kv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kv4 OCA], [https://pdbe.org/7kv4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kv4 RCSB], [https://www.ebi.ac.uk/pdbsum/7kv4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kv4 ProSAT]</span></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=7kv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kv4 OCA], [https://pdbe.org/7kv4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kv4 RCSB], [https://www.ebi.ac.uk/pdbsum/7kv4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kv4 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/F3PPH4_9BACE F3PPH4_9BACE]
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Complex glycans that evade our digestive system are major nutrients that feed the human gut microbiota (HGM). The prevalence of Bacteroidetes in the HGM of populations worldwide is engendered by the evolution of Polysaccharide Utilization Locus (PUL), which encode concerted protein systems to utilize the myriad complex glycans in our diets. Despite their crucial roles in glycan recognition and transport, cell-surface glycan-binding proteins (SGBPs) remained understudied cogs in the PUL machinery. Here, we report the structural and biochemical characterization of a suite of SGBP-A and SGBP-B structures from three syntenic beta(1,3)-glucan utilization loci (1,3GULs) from Bacteroides thetaiotaomicron (Bt), B. uniformis (Bu), and B. fluxus (Bf), which have varying specificities for distinct beta-glucans. Ligand complexes provide definitive insight into beta(1,3)-glucan selectivity in the HGM, including structural features enabling dual beta(1,3)-glucan/mixed-linkage beta(1,3)/beta(1,4)-glucan binding capability in some orthologs. The tertiary structural conservation of SusD-like SGBPs-A is juxtaposed with the diverse architectures and binding modes of the SGBPs-B. Specifically, the structures of the tri-modular BtSGBP-B and BuSGBP-B revealed a tandem repeat of Carbohydrate-Binding Module-Like domains connected by long linkers. In contrast, BfSGBP-B comprises a bi-modular architecture with a distinct beta-barrel domain at the C-terminus that bears a shallow binding canyon. The molecular insights obtained here contribute to our fundamental understanding of HGM function, which in turn may inform tailored microbial intervention therapies.
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Distinct protein architectures mediate species-specific beta-glucan binding and metabolism in the human gut microbiota.,Tamura K, Dejean G, Van Petegem F, Brumer H J Biol Chem. 2021 Feb 12:100415. doi: 10.1016/j.jbc.2021.100415. PMID:33587952<ref>PMID:33587952</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 7kv4" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacteroides fluxus dsm 22534]]
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[[Category: Bacteroides fluxus YIT 12057]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Brumer, H]]
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[[Category: Brumer H]]
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[[Category: Petegem, F Van]]
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[[Category: Tamura K]]
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[[Category: Tamura, K]]
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[[Category: Van Petegem F]]
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[[Category: Cbm]]
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[[Category: Sugar binding protein]]
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[[Category: Susd]]
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[[Category: Tetratricopeptide repeat]]
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Current revision

Surface glycan-binding protein A from Bacteroides fluxus

PDB ID 7kv4

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