6S0E
Crystal structure of an inverting family GH156 exosialidase from uncultured bacterium pG7 in complex with N-Acetyl-2,3-dehydro-2-deoxyneuraminic acid
Summary for 6S0E
| Entry DOI | 10.2210/pdb6s0e/pdb |
| Descriptor | exosialidase from uncultured bacterium pG7, GLYCEROL, ACETATE ION, ... (7 entities in total) |
| Functional Keywords | (beta/alpha )8 barrel, hydrolase, sialidase, inverting, homodimer |
| Biological source | uncultured bacterium pG7 |
| Total number of polymer chains | 2 |
| Total formula weight | 119534.18 |
| Authors | Bule, P.,Blagova, E.,Chuzel, L.,Taron, C.H.,Davies, G.J. (deposition date: 2019-06-14, release date: 2019-11-06, Last modification date: 2024-01-24) |
| Primary citation | Bule, P.,Chuzel, L.,Blagova, E.,Wu, L.,Gray, M.A.,Henrissat, B.,Rapp, E.,Bertozzi, C.R.,Taron, C.H.,Davies, G.J. Inverting family GH156 sialidases define an unusual catalytic motif for glycosidase action. Nat Commun, 10:4816-4816, 2019 Cited by PubMed Abstract: Sialic acids are a family of related sugars that play essential roles in many biological events intimately linked to cellular recognition in both health and disease. Sialidases are therefore orchestrators of cellular biology and important therapeutic targets for viral infection. Here, we sought to define if uncharacterized sialidases would provide distinct paradigms in sialic acid biochemistry. We show that a recently discovered sialidase family, whose first member EnvSia156 was isolated from hot spring metagenomes, defines an unusual structural fold and active centre constellation, not previously described in sialidases. Consistent with an inverting mechanism, EnvSia156 reveals a His/Asp active center in which the His acts as a Brønsted acid and Asp as a Brønsted base in a single-displacement mechanism. A predominantly hydrophobic aglycone site facilitates accommodation of a variety of 2-linked sialosides; a versatility that offers the potential for glycan hydrolysis across a range of biological and technological platforms. PubMed: 31645552DOI: 10.1038/s41467-019-12684-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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