6fuv

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<StructureSection load='6fuv' size='340' side='right'caption='[[6fuv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='6fuv' size='340' side='right'caption='[[6fuv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6fuv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FUV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FUV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6fuv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bifidibacterium"_prevot_1938 "bifidibacterium" prevot 1938]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FUV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FUV FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=P33:3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL'>P33</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=P33:3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL'>P33</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Blac_00785 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1678 "Bifidibacterium" Prevot 1938])</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=6fuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fuv OCA], [http://pdbe.org/6fuv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fuv RCSB], [http://www.ebi.ac.uk/pdbsum/6fuv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fuv 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=6fuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fuv OCA], [http://pdbe.org/6fuv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fuv RCSB], [http://www.ebi.ac.uk/pdbsum/6fuv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fuv ProSAT]</span></td></tr>
</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 bifidobacteria rely on ATP-binding cassette (ABC) transporters for oligosaccharide uptake. Multiple oligosaccharide-specific solute binding protein (SBP) genes are occasionally associated with a single ABC transporter, but the significance of this multiplicity remains unclear. Here, we characterize BlMnBP1 and BlMnBP2, the two SBPs associated to the beta-manno-oligosaccharide (MnOS) ABC transporter in Bifidobacterium animalis subsp. lactis. Despite similar overall specificity and preference to mannotriose (Kd approximately 80 nM), affinity of BlMnBP1 is up to 2570-fold higher for disaccharides than BlMnBP2. Structural analysis revealed a substitution of an asparagine that recognizes the mannosyl at position 2 in BlMnBP1, by a glycine in BlMnBP2, which affects substrate affinity. Both substitution-types occur in bifidobacterial SBPs, but BlMnBP1-like variants prevail in human-gut isolates. B. animalis subsp. lactis ATCC27673 showed growth on gluco- and galactomannans and was able to outcompete a mannan-degrading Bacteroides ovatus strain in co-cultures, attesting the efficiency of this ABC uptake system. By contrast, a strain that lacks this transporter failed to grow on mannan. This study highlights SBP diversification as a possible strategy to modulate oligosaccharide uptake preferences of bifidobacterial ABC-transporters during adaptation to specific ecological niches. Efficient metabolism of galactomannan by distinct bifidobacteria, merits evaluating this plant glycan as a potential prebiotic. This article is protected by copyright. All rights reserved.
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Two binding proteins of the ABC transporter that confers growth of Bifidobacterium animalis subsp. lactis ATCC27673 on beta-mannan possess distinct manno-oligosaccharide binding profiles.,Ejby M, Guskov A, Pichler MJ, Zanten GC, Schoof E, Saburi W, Slotboom DJ, Abou Hachem M Mol Microbiol. 2019 Apr 4. doi: 10.1111/mmi.14257. PMID:30947380<ref>PMID:30947380</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 6fuv" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bifidibacterium prevot 1938]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ejby, M]]
[[Category: Ejby, M]]

Revision as of 06:48, 17 April 2019

Structure of a manno-oligosaccharide specific solute binding protein, BlMnBP2 from Bifidobacterium animalis subsp. lactis ATCC 27673 in complex with mannotriose

PDB ID 6fuv

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