This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3sli

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="3sli" size="450" color="white" frame="true" align="right" spinBox="true" caption="3sli, resolution 1.8&Aring;" /> '''LEECH INTRAMOLECULAR ...)
Line 1: Line 1:
-
[[Image:3sli.gif|left|200px]]<br /><applet load="3sli" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:3sli.gif|left|200px]]<br /><applet load="3sli" size="350" color="white" frame="true" align="right" spinBox="true"
caption="3sli, resolution 1.8&Aring;" />
caption="3sli, resolution 1.8&Aring;" />
'''LEECH INTRAMOLECULAR TRANS-SIALIDASE COMPLEXED WITH 2,7-ANHYDRO-NEU5AC PREPARED BY SOAKING WITH 3'-SIALYLLACTOSE'''<br />
'''LEECH INTRAMOLECULAR TRANS-SIALIDASE COMPLEXED WITH 2,7-ANHYDRO-NEU5AC PREPARED BY SOAKING WITH 3'-SIALYLLACTOSE'''<br />
==Overview==
==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.
+
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==
-
3SLI 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 SKD 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=3SLI OCA].
+
3SLI 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=SKD:'>SKD</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=3SLI OCA].
==Reference==
==Reference==
Line 14: Line 14:
[[Category: Macrobdella decora]]
[[Category: Macrobdella decora]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Li, S.C.]]
+
[[Category: Li, S C.]]
-
[[Category: Li, Y.T.]]
+
[[Category: Li, Y T.]]
[[Category: Luo, M.]]
[[Category: Luo, M.]]
[[Category: Luo, Y.]]
[[Category: Luo, Y.]]
Line 23: Line 23:
[[Category: neuraminidase]]
[[Category: neuraminidase]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:58:50 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:11:22 2008''

Revision as of 17:11, 21 February 2008


3sli, resolution 1.8Å

Drag the structure with the mouse to rotate

LEECH INTRAMOLECULAR TRANS-SIALIDASE COMPLEXED WITH 2,7-ANHYDRO-NEU5AC PREPARED BY SOAKING WITH 3'-SIALYLLACTOSE

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

3SLI 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

Page seeded by OCA on Thu Feb 21 19:11:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools