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Article Dans Une Revue Acta crystallographica Section D : Structural biology [1993-...] Année : 2015

Structural bases for N-glycan processing by mannoside phosphorylase

Résumé

The first crystal structure of Uhgb_MP, a β-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 Å 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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Cristallographie
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Dates et versions

hal-01183896 , version 1 (11-08-2015)

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Simon Ladeveze, Gianluca Cioci, Pierre Roblin, Lionel Mourey, Samuel Tranier, et al.. Structural bases for N-glycan processing by mannoside phosphorylase. Acta crystallographica Section D : Structural biology [1993-..], 2015, 71 (Part 6), pp.1335-46. ⟨10.1107/S1399004715006604⟩. ⟨hal-01183896⟩
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