View source for 5bxp


==LNBase in complex with LNB-LOGNAc==
<StructureSection load='5bxp' size='340' side='right'caption='[[5bxp]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5bxp]] 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=5BXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BXP 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]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=LOG:LOGNAC'>LOG</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=5bxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bxp OCA], [https://pdbe.org/5bxp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bxp RCSB], [https://www.ebi.ac.uk/pdbsum/5bxp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bxp 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 ==
The synthesis of potent inhibitors for lacto-N-biosidases and X-ray structural characterization of these compounds in complex with BbLNBase is described.

Gaining insight into the catalysis by GH20 lacto-N-biosidase using small molecule inhibitors and structural analysis.,Hattie M, Ito T, Debowski AW, Arakawa T, Katayama T, Yamamoto K, Fushinobu S, Stubbs KA Chem Commun (Camb). 2015 Aug 27. PMID:26312778<ref>PMID:26312778</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5bxp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bifidobacterium bifidum JCM 1254]]
[[Category: Large Structures]]
[[Category: Arakawa T]]
[[Category: Fushinobu S]]
[[Category: Ito T]]