4UDI
Crystal structure of b-1,4-mannopyranosyl-chitobiose phosphorylase at 1.85 Angstrom from unknown human gut bacteria (Uhgb_MP)
Summary for 4UDI
Entry DOI | 10.2210/pdb4udi/pdb |
Related | 4UDG 4UDJ 4UDK |
Descriptor | UHGB_MP, PHOSPHATE ION, GLYCEROL, ... (7 entities in total) |
Functional Keywords | transferase, glycoside hydrolase family 130, b-1, 4-mannopyranosyl-chitobiose phosphorylase, n-glycan phosphorolysis |
Biological source | UNCULTURED ORGANISM |
Total number of polymer chains | 6 |
Total formula weight | 240973.43 |
Authors | Ladeveze, S.,Cioci, G.,Potocki-Veronese, G.,Tranier, S.,Mourey, L. (deposition date: 2014-12-10, release date: 2015-05-27, Last modification date: 2023-12-20) |
Primary citation | Ladeveze, S.,Cioci, G.,Roblin, P.,Mourey, L.,Tranier, S.,Potocki-Veronese, G. Structural Bases for N-Glycan Processing by Mannoside Phosphorylase. Acta Crystallogr.,Sect.D, 71:1335-, 2015 Cited by PubMed Abstract: 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. PubMed: 26057673DOI: 10.1107/S1399004715006604 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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