4sli

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{{STRUCTURE_4sli| PDB=4sli | SCENE= }}
{{STRUCTURE_4sli| PDB=4sli | SCENE= }}
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'''LEECH INTRAMOLECULAR TRANS-SIALIDASE COMPLEXED WITH 2-PROPENYL-NEU5AC, AN INACTIVE SUBSTRATE ANALOGUE'''
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===LEECH INTRAMOLECULAR TRANS-SIALIDASE COMPLEXED WITH 2-PROPENYL-NEU5AC, AN INACTIVE SUBSTRATE ANALOGUE===
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==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.
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{{ABSTRACT_PUBMED_9878409}}
==About this Structure==
==About this Structure==
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[[Category: Enzyme]]
[[Category: Enzyme]]
[[Category: Intramolecular trans-sialidase]]
[[Category: Intramolecular trans-sialidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:29:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:50:49 2008''

Revision as of 10:50, 3 July 2008

Image:4sli.png

Template:STRUCTURE 4sli

LEECH INTRAMOLECULAR TRANS-SIALIDASE COMPLEXED WITH 2-PROPENYL-NEU5AC, AN INACTIVE SUBSTRATE ANALOGUE

Template:ABSTRACT PUBMED 9878409

About this Structure

4SLI is a Single protein structure of sequence from Macrobdella decora. Full crystallographic information is available from OCA.

Reference

The 1.8 A structures of leech intramolecular trans-sialidase complexes: evidence of its enzymatic mechanism., Luo Y, Li SC, Li YT, Luo M, J Mol Biol. 1999 Jan 8;285(1):323-32. PMID:9878409

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