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| <StructureSection load='5gqf' size='340' side='right'caption='[[5gqf]], [[Resolution|resolution]] 1.82Å' scene=''> | | <StructureSection load='5gqf' size='340' side='right'caption='[[5gqf]], [[Resolution|resolution]] 1.82Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[5gqf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GQF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5GQF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5gqf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bifidobacterium_longum_subsp._longum Bifidobacterium longum subsp. longum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GQF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GQF FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 1.82Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gqc|5gqc]], [[5gqg|5gqg]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lacto-N-biosidase Lacto-N-biosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.140 3.2.1.140] </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=5gqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gqf OCA], [https://pdbe.org/5gqf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gqf RCSB], [https://www.ebi.ac.uk/pdbsum/5gqf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gqf ProSAT]</span></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5gqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gqf OCA], [http://pdbe.org/5gqf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gqf RCSB], [http://www.ebi.ac.uk/pdbsum/5gqf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gqf ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/A0A024QYS6_BIFLN A0A024QYS6_BIFLN] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Lacto-N-biosidase]] | + | [[Category: Bifidobacterium longum subsp. longum]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Arakawa, T]] | + | [[Category: Arakawa T]] |
- | [[Category: Fushinobu, S]] | + | [[Category: Fushinobu S]] |
- | [[Category: Katayama, T]] | + | [[Category: Katayama T]] |
- | [[Category: Yamada, C]] | + | [[Category: Yamada C]] |
- | [[Category: Beta-helix]]
| + | |
- | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
A0A024QYS6_BIFLN
Publication Abstract from PubMed
Breast-fed infants generally have a bifidobacteria-rich microbiota with recent studies indicating that human milk oligosaccharides (HMOs) selectively promote bifidobacterial growth. Bifidobacterium bifidum possesses a glycoside hydrolase family 20 lacto-N-biosidase for liberating lacto-N-biose I from lacto-N-tetraose, an abundant HMO unique to human milk, while Bifidobacterium longum subsp. longum has a non-classified enzyme (LnbX). Here, we determined the crystal structure of the catalytic domain of LnbX and provide evidence for creation of a novel glycoside hydrolase family, GH136. The structure, in combination with inhibition and mutation studies, provides insight into the molecular mechanism and broader substrate specificity of this enzyme. Moreover, through genetic studies, we show that lnbX is indispensable for B. longum growth on lacto-N-tetraose and is a key genetic factor for persistence in the gut of breast-fed infants. Overall, this study reveals possible evolutionary routes for the emergence of symbiosis between humans and bifidobacterial species in the infant gut.
Molecular Insight into Evolution of Symbiosis between Breast-Fed Infants and a Member of the Human Gut Microbiome Bifidobacterium longum.,Yamada C, Gotoh A, Sakanaka M, Hattie M, Stubbs KA, Katayama-Ikegami A, Hirose J, Kurihara S, Arakawa T, Kitaoka M, Okuda S, Katayama T, Fushinobu S Cell Chem Biol. 2017 Apr 4. pii: S2451-9456(17)30095-8. doi:, 10.1016/j.chembiol.2017.03.012. PMID:28392148[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yamada C, Gotoh A, Sakanaka M, Hattie M, Stubbs KA, Katayama-Ikegami A, Hirose J, Kurihara S, Arakawa T, Kitaoka M, Okuda S, Katayama T, Fushinobu S. Molecular Insight into Evolution of Symbiosis between Breast-Fed Infants and a Member of the Human Gut Microbiome Bifidobacterium longum. Cell Chem Biol. 2017 Apr 4. pii: S2451-9456(17)30095-8. doi:, 10.1016/j.chembiol.2017.03.012. PMID:28392148 doi:http://dx.doi.org/10.1016/j.chembiol.2017.03.012
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