2sli: Difference between revisions

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[[Image:2sli.gif|left|200px]]
{{Seed}}
[[Image:2sli.png|left|200px]]


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{{STRUCTURE_2sli|  PDB=2sli  |  SCENE=  }}  
{{STRUCTURE_2sli|  PDB=2sli  |  SCENE=  }}  


'''LEECH INTRAMOLECULAR TRANS-SIALIDASE COMPLEXED WITH 2,7-ANHYDRO-NEU5AC, THE REACTION PRODUCT'''
===LEECH INTRAMOLECULAR TRANS-SIALIDASE COMPLEXED WITH 2,7-ANHYDRO-NEU5AC, THE REACTION PRODUCT===




==Overview==
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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--&gt;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.
The line below this paragraph, {{ABSTRACT_PUBMED_9878409}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_9878409}}


==About this Structure==
==About this Structure==
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[[Category: Intramolecular trans-sialidase]]
[[Category: Intramolecular trans-sialidase]]
[[Category: Neuraminidase]]
[[Category: Neuraminidase]]
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