4udg

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4udg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4udg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4udg RCSB], [http://www.ebi.ac.uk/pdbsum/4udg PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4udg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4udg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4udg RCSB], [http://www.ebi.ac.uk/pdbsum/4udg PDBsum]</span></td></tr>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 09:00, 17 June 2015

Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.60 Angstrom in complex with N-acetylglucosamine and inorganic phosphate

4udg, resolution 1.60Å

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