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5bxt
From Proteopedia
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==LNBase in complex with LNB-NHAcAUS== | ==LNBase in complex with LNB-NHAcAUS== | ||
| - | <StructureSection load='5bxt' size='340' side='right' caption='[[5bxt]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='5bxt' size='340' side='right'caption='[[5bxt]], [[Resolution|resolution]] 1.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5bxt]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BXT OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5bxt]] 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=5BXT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BXT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4WS:N-{[(1R,2R,3R,7S,7AR)-1,2,7-TRIHYDROXYHEXAHYDRO-1H-PYRROLIZIN-3-YL]METHYL}ACETAMIDE'>4WS</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4WS:N-{[(1R,2R,3R,7S,7AR)-1,2,7-TRIHYDROXYHEXAHYDRO-1H-PYRROLIZIN-3-YL]METHYL}ACETAMIDE'>4WS</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5bxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bxt OCA], [https://pdbe.org/5bxt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bxt RCSB], [https://www.ebi.ac.uk/pdbsum/5bxt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bxt ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Bifidobacterium bifidum JCM 1254]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Arakawa T]] |
| - | + | [[Category: Fushinobu S]] | |
| - | [[Category: | + | [[Category: Ito T]] |
| - | [[Category: | + | |
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Current revision
LNBase in complex with LNB-NHAcAUS
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