2SLI
LEECH INTRAMOLECULAR TRANS-SIALIDASE COMPLEXED WITH 2,7-ANHYDRO-NEU5AC, THE REACTION PRODUCT
Summary for 2SLI
| Entry DOI | 10.2210/pdb2sli/pdb |
| Descriptor | INTRAMOLECULAR TRANS-SIALIDASE, 2-ACETYLAMINO-7-(1,2-DIHYDROXY-ETHYL)-3-HYDROXY-6,8-DIOXA-BICYCLO[3.2.1]OCTANE-5-CARBOXYLIC ACID (3 entities in total) |
| Functional Keywords | hydrolase, intramolecular trans-sialidase, neuraminidase |
| Biological source | Macrobdella decora (North American leech) |
| Cellular location | Secreted, extracellular space: Q27701 |
| Total number of polymer chains | 1 |
| Total formula weight | 74856.94 |
| Authors | |
| Primary citation | Luo, Y.,Li, S.C.,Li, Y.T.,Luo, M. The 1.8 A structures of leech intramolecular trans-sialidase complexes: evidence of its enzymatic mechanism. J.Mol.Biol., 285:323-332, 1999 Cited by PubMed Abstract: Intramolecular trans-sialidase from leech (Macrobdella decora) is the first member of the sialidase superfamily found to exhibit strict specificity towards the cleavage of terminal Neu5Acalpha2-->3Gal linkage in sialoglycoconjugates. Its release of 2,7-anhydro-Neu5Ac instead of Neu5Ac indicates that it catalyzes an intramolecular trans-sialosyl reaction. Crystal structures of its complexes with an inactive substrate analogue 2-propenyl-Neu5Ac, and with the product 2,7-anhydro-Neu5Ac, have been determined to 1.8 A resolution. The boat conformation of the pyranose observed in the complexes supports the proposed enzymatic mechanism that O7 of an axial 6-glycerol group attacks the positively charged C2 of the intermediate. A generalized mechanism is proposed for the sialidase superfamily. PubMed: 9878409DOI: 10.1006/jmbi.1998.2345 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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