View source for 4udg


==Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.60 Angstrom in complex with N-acetylglucosamine and inorganic phosphate==
<StructureSection load='4udg' size='340' side='right'caption='[[4udg]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4udg]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Uncultured_organism Uncultured organism]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UDG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UDG 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]] 1.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=4udg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4udg OCA], [https://pdbe.org/4udg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4udg RCSB], [https://www.ebi.ac.uk/pdbsum/4udg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4udg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D9ZDQ9_9ZZZZ D9ZDQ9_9ZZZZ] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The first crystal structure of Uhgb_MP, a beta-1,4-mannopyranosyl-chitobiose phosphorylase belonging to the GH130 family which is involved in N-glycan degradation by human gut bacteria, was solved at 1.85 A resolution in the apo form and in complex with mannose and N-acetylglucosamine. SAXS and crystal structure analysis revealed a hexameric structure, a specific feature of GH130 enzymes among other glycoside phosphorylases. Mapping of the -1 and +1 subsites in the presence of phosphate confirmed the conserved Asp104 as the general acid/base catalytic residue, which is in agreement with a single-step reaction mechanism involving Man O3 assistance for proton transfer. Analysis of this structure, the first to be solved for a member of the GH130_2 subfamily, revealed Met67, Phe203 and the Gly121-Pro125 loop as the main determinants of the specificity of Uhgb_MP and its homologues towards the N-glycan core oligosaccharides and mannan, and the molecular bases of the key role played by GH130 enzymes in the catabolism of dietary fibre and host glycans.

Structural bases for N-glycan processing by mannoside phosphorylase.,Ladeveze S, Cioci G, Roblin P, Mourey L, Tranier S, Potocki-Veronese G Acta Crystallogr D Biol Crystallogr. 2015 Jun;71(Pt 6):1335-46. doi:, 10.1107/S1399004715006604. Epub 2015 May 14. PMID:26057673<ref>PMID:26057673</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4udg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Uncultured organism]]
[[Category: Cioci G]]
[[Category: Ladeveze S]]
[[Category: Mourey L]]
[[Category: Potocki-Veronese G]]
[[Category: Tranier S]]