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1SLI

LEECH INTRAMOLECULAR TRANS-SIALIDASE COMPLEXED WITH DANA

Summary for 1SLI
Entry DOI10.2210/pdb1sli/pdb
DescriptorINTRAMOLECULAR TRANS-SIALIDASE, 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID (3 entities in total)
Functional Keywordshydrolase, intramolecular trans-sialidase, neuraminidase
Biological sourceMacrobdella decora (North American leech)
Cellular locationSecreted, extracellular space: Q27701
Total number of polymer chains1
Total formula weight74856.94
Authors
Luo, Y.,Li, S.C.,Chou, M.Y.,Li, Y.T.,Luo, M. (deposition date: 1998-03-28, release date: 1999-04-20, Last modification date: 2024-04-03)
Primary citationLuo, Y.,Li, S.C.,Chou, M.Y.,Li, Y.T.,Luo, M.
The crystal structure of an intramolecular trans-sialidase with a NeuAc alpha2-->3Gal specificity.
Structure, 6:521-530, 1998
Cited by
PubMed Abstract: Intramolecular trans-sialidase from leech (Macrobdella decora) is a unique enzyme which cleaves the terminal neuraminic acid (NeuAc) residue from sialoglycoconjugates, releasing 2, 7-anhydro-neuraminic acid (2,7-anhydro-NeuAc). It is the first enzyme found to exhibit strictly specific cleavage of NeuAc alpha2-->3Gal linkages in sialoglycoconjugates. The release of 2,7-anhydro-NeuAc instead of NeuAc implies a unique mechanism, in which the sialosyl linkage is transferred within the sialoglycoconjugate rather than hydrolyzed. The aims of the structural study were to gain structural insight into the strict specificity and unique mechanism of this unusual enzyme.
PubMed: 9562562
DOI: 10.1016/S0969-2126(98)00053-7
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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