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6RZD

Crystal structure of an inverting family GH156 exosialidase from uncultured bacterium pG7

Summary for 6RZD
Entry DOI10.2210/pdb6rzd/pdb
Descriptorexosialidase from uncultured bacterium pG7, SULFATE ION, TRIS(HYDROXYETHYL)AMINOMETHANE, ... (6 entities in total)
Functional Keywords(beta/alpha )8 barrel, hydrolase, sialidase, inverting, homodimer
Biological sourceuncultured bacterium pG7
Total number of polymer chains2
Total formula weight119208.85
Authors
Bule, P.,Blagova, E.,Chuzel, L.,Taron, C.H.,Davies, G.J. (deposition date: 2019-06-13, release date: 2019-11-06, Last modification date: 2024-05-01)
Primary citationBule, 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: 31645552
DOI: 10.1038/s41467-019-12684-7
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

227561

数据于2024-11-20公开中

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