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9wfh
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Carbohydrate-binding module 32 of LnbB from Bifidobacterium bifidum, ligand free form, multiple small-wedge data set== | |
| + | <StructureSection load='9wfh' size='340' side='right'caption='[[9wfh]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9wfh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bifidobacterium_bifidum_JCM_1254 Bifidobacterium bifidum JCM 1254]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9WFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9WFH FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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></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=9wfh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9wfh OCA], [https://pdbe.org/9wfh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9wfh RCSB], [https://www.ebi.ac.uk/pdbsum/9wfh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9wfh ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/LNBB_BIFB1 LNBB_BIFB1] Present in the infant gut, this enzyme is involved in the assimilation of type-1 human milk oligosaccharides (HMOs). It hydrolyzes via a retaining mechanism the beta-D-GlcNAc-(1->3)-beta-D-Gal linkage in lacto-N-tetraose (LNT or beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc), an abundant HMO unique to human breast milk, releasing lacto-N-biose (LNB or beta-D-Gal-(1->3)-D-GlcNAc) and lactose (PubMed:18469123, PubMed:23479733). Is a key enzymatic factor for growth and proliferation of B.bifidum in the gut ecosystem of breast-fed infants (Probable). Has substrate preference for unmodified beta-linked LNB since it does not hydrolyze the fucosylated forms of lacto-N-tetraose (lacto-N-fucopentaose I and II) or lacto-N-neotetraose. Is also able to display transglycosylation activity in vitro (PubMed:18469123).<ref>PMID:18469123</ref> <ref>PMID:23479733</ref> <ref>PMID:23479733</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bifidobacterium bifidum, a predominant colonizer of the infant gut, utilizes lacto-N-biose I (LNB), a prominent component of human milk oligosaccharides (HMOs), through a dedicated metabolic pathway. Among a diverse set of extracellular glycosidases involved in HMO degradation, lacto-N-biosidase (LnbB) plays a pivotal role by releasing LNB. We investigated the structure and function of the carbohydrate-binding module family 32 (CBM32) domain located at the C-terminus of the glycoside hydrolase family 20 catalytic domain in LnbB. Isothermal titration calorimetry showed that CBM32 binds LNB with a dissociation constant (K(d)) of 98 mum. The crystal structure of the CBM32 complexed with LNB reveals the molecular basis for its specific recognition. Impact statement Bifidobacteria are beneficial gut microbes, and infant-associated strains establish symbiosis by degrading human milk oligosaccharides. This study uncovers the molecular mechanism by which Bifidobacterium bifidum captures lacto-N-biose I, a key disaccharide, functioning as a cross-feeder that promotes the growth of other bifidobacteria and supports the infant gut ecosystem. | ||
| - | + | Structural insights into lacto-N-biose I recognition by a family 32 carbohydrate-binding module from Bifidobacterium bifidum.,Zhang X, Sunagawa N, Kashima T, Igarashi K, Miyanaga A, Fushinobu S FEBS Lett. 2025 Nov 7. doi: 10.1002/1873-3468.70217. PMID:41204437<ref>PMID:41204437</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9wfh" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bifidobacterium bifidum JCM 1254]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Fushinobu S]] | ||
| + | [[Category: Kashima T]] | ||
| + | [[Category: Zhang X]] | ||
Current revision
Carbohydrate-binding module 32 of LnbB from Bifidobacterium bifidum, ligand free form, multiple small-wedge data set
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