4sli: Difference between revisions

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[[Image:4sli.~~jpg~~|left|200px]]

[[Image:4sli.png|left|200px]]

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

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

~~==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~~-~~->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

(as it appears on PubMed at http://www.pubmed.gov), where 9878409 is the PubMed ID number.

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==About this Structure==

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[[Category: Enzyme]]

[[Category: Intramolecular trans-sialidase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May~~ ~~4 22~~:29:33 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:50:49 2008''

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-[[Image:4sli.jpg|left|200px]]
+{{Seed}}
+[[Image:4sli.png|left|200px]]
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 {{STRUCTURE_4sli|  PDB=4sli  |  SCENE=  }}
-'''LEECH INTRAMOLECULAR TRANS-SIALIDASE COMPLEXED WITH 2-PROPENYL-NEU5AC, AN INACTIVE SUBSTRATE ANALOGUE'''
+===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--&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
+(as it appears on PubMed at http://www.pubmed.gov), where 9878409 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9878409}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Enzyme]]
 [[Category: Intramolecular trans-sialidase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:29:33 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul  3 13:50:49 2008''