View source for 9fyl


==Lacto-N-biosidase from Treponema denticola ATCC 35405, HisTag bound in active site==
<StructureSection load='9fyl' size='340' side='right'caption='[[9fyl]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9fyl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Treponema_denticola_ATCC_35405 Treponema denticola ATCC 35405]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9FYL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9FYL 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]] 2.24&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=9fyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9fyl OCA], [https://pdbe.org/9fyl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9fyl RCSB], [https://www.ebi.ac.uk/pdbsum/9fyl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9fyl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q73LY9_TREDE Q73LY9_TREDE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The glycoside hydrolase family 20 (GH20) predominantly features N-acetylhexosaminidases (EC 3.2.1.52), with only few known lacto-N-biosidases (EC 3.2.1.140; LNBases). LNBases catalyze the degradation of lacto-N-tetraose (LNT), a prominent component of human milk oligosaccharides, thereby supporting a healthy infant gut microbiome development. We investigated GH20 diversity to discover novel enzymes that release disaccharides such as lacto-N-biose (LNB). Our approach combined peptide clustering, sequence analysis, and 3D structure model evaluation to assess active site topologies, focusing on the presence of a subsite -2. Five LNBases were active on pNP-LNB and four showed activity on LNT. One enzyme displayed activity on both pNP-LacNAc and pNP-LNB, establishing the first report of N-acetyllactosaminidase (LacNAcase) activity. Exploration of this enzyme cluster led to the identification of four additional enzymes sharing this dual substrate specificity. Comparing the determined crystal structure of a specific LNBase (TrpyGH20) and the first crystal structure of an enzyme with dual LacNAcase/LNBase activity (TrdeGH20) revealed a highly conserved subsite -1, common to GH20 enzymes, while the -2 subsites varied significantly. TrdeGH20 had a wider subsite -2, accommodating Gal with both beta1,4- and beta1,3-linkages to the GlcNAc in subsite -1. Biotechnological applications of these enzymes may include structural elucidation of complex carbohydrates and glycoengineering.

Discovery of Lacto-N-biosidases and a Novel N-Acetyllactosaminidase Activity in the CAZy Family GH20: Functional Diversity and Structural Insights.,Vuillemin M, Muschiol J, Zhang Y, Holck J, Barrett K, Morth JP, Meyer AS, Zeuner B Chembiochem. 2024 Sep 6:e202400710. doi: 10.1002/cbic.202400710. PMID:39239753<ref>PMID:39239753</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9fyl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Treponema denticola ATCC 35405]]
[[Category: Morth JP]]
[[Category: Siebenhaar S]]
[[Category: Vuillemin M]]
[[Category: Zeuner B]]