4sli

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(New page: 200px<br /><applet load="4sli" size="450" color="white" frame="true" align="right" spinBox="true" caption="4sli, resolution 1.8&Aring;" /> '''LEECH INTRAMOLECULAR ...)
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[[Image:4sli.jpg|left|200px]]<br /><applet load="4sli" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:4sli.jpg|left|200px]]<br /><applet load="4sli" size="350" color="white" frame="true" align="right" spinBox="true"
caption="4sli, resolution 1.8&Aring;" />
caption="4sli, resolution 1.8&Aring;" />
'''LEECH INTRAMOLECULAR TRANS-SIALIDASE COMPLEXED WITH 2-PROPENYL-NEU5AC, AN INACTIVE SUBSTRATE ANALOGUE'''<br />
'''LEECH INTRAMOLECULAR TRANS-SIALIDASE COMPLEXED WITH 2-PROPENYL-NEU5AC, AN INACTIVE SUBSTRATE ANALOGUE'''<br />
==Overview==
==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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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.
==About this Structure==
==About this Structure==
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4SLI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Macrobdella_decora Macrobdella decora] with CNP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4SLI OCA].
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4SLI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Macrobdella_decora Macrobdella decora] with <scene name='pdbligand=CNP:'>CNP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4SLI OCA].
==Reference==
==Reference==
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[[Category: Macrobdella decora]]
[[Category: Macrobdella decora]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Li, S.C.]]
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[[Category: Li, S C.]]
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[[Category: Li, Y.T.]]
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[[Category: Li, Y T.]]
[[Category: Luo, M.]]
[[Category: Luo, M.]]
[[Category: Luo, Y.]]
[[Category: Luo, Y.]]
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[[Category: intramolecular trans-sialidase]]
[[Category: intramolecular trans-sialidase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:48:22 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:14:24 2008''

Revision as of 17:14, 21 February 2008


4sli, resolution 1.8Å

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

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

4SLI is a Single protein structure of sequence from Macrobdella decora with 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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