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2sli

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(New page: 200px<br /><applet load="2sli" size="450" color="white" frame="true" align="right" spinBox="true" caption="2sli, resolution 1.8&Aring;" /> '''LEECH INTRAMOLECULAR ...)
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Revision as of 11:54, 21 November 2007

Image:2sli.gif

2sli, resolution 1.8Å

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

Overview

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.

About this Structure

2SLI is a Single protein structure of sequence from Macrobdella decora with SKD as ligand. Active as Exo-alpha-sialidase, with EC number 3.2.1.18 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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